STRINGSTRING
EKF06090.1 EKF06090.1 EKF05883.1 EKF05883.1 EKF05885.1 EKF05885.1 EKF05888.1 EKF05888.1 ndhH ndhH EKF05805.1 EKF05805.1 EKF05806.1 EKF05806.1 EKF05849.1 EKF05849.1 EKF05858.1 EKF05858.1 EKF05859.1 EKF05859.1 EKF04686.1 EKF04686.1 EKF04903.1 EKF04903.1 EKF05194.1 EKF05194.1 EKF05314.1 EKF05314.1 EKF05343.1 EKF05343.1 EKF04498.1 EKF04498.1 EKF04499.1 EKF04499.1 EKF04500.1 EKF04500.1 EKF03810.1 EKF03810.1 EKF03728.1 EKF03728.1 ndhD ndhD EKF03486.1 EKF03486.1 ndhD-2 ndhD-2 EKF03253.1 EKF03253.1 EKF03277.1 EKF03277.1 ndhC ndhC ndhK ndhK ndhJ ndhJ EKE98666.1 EKE98666.1 EKE98668.1 EKE98668.1 EKE98669.1 EKE98669.1 EKE98764.1 EKE98764.1 ctaB ctaB EKE98778.1 EKE98778.1 EKE98779.1 EKE98779.1 EKE98780.1 EKE98780.1 EKE98781.1 EKE98781.1 EKE98576.1 EKE98576.1 ndhO ndhO EKE98164.1 EKE98164.1 EKE97812.1 EKE97812.1 EKE97830.1 EKE97830.1 EKE97831.1 EKE97831.1 EKE97833.1 EKE97833.1 EKE97463.1 EKE97463.1 EKE97464.1 EKE97464.1 petC petC EKF03214.1 EKF03214.1 EKF02929.1 EKF02929.1 EKF02676.1 EKF02676.1 ndhN ndhN EKF02047.1 EKF02047.1 EKF02048.1 EKF02048.1 EKF02050.1 EKF02050.1 EKF02096.1 EKF02096.1 EKF01942.1 EKF01942.1 EKF01467.1 EKF01467.1 EKF01392.1 EKF01392.1 EKF01264.1 EKF01264.1 EKF01265.1 EKF01265.1 EKF01164.1 EKF01164.1 EKF01024.1 EKF01024.1 EKF00538.1 EKF00538.1 EKF00710.1 EKF00710.1 ndhD-3 ndhD-3 EKF00324.1 EKF00324.1 EKF00356.1 EKF00356.1 EKF00357.1 EKF00357.1 EKF00360.1 EKF00360.1 ndhB ndhB EKF00214.1 EKF00214.1 ndhE ndhE EKE99675.1 EKE99675.1 ndhI ndhI ndhA ndhA EKE99495.1 EKE99495.1 EKE99498.1 EKE99498.1 ndhM ndhM
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
EKF06090.1beta-Ig-H3/fasciclin family protein; KEGG: ade:Adeh_2131 0.14 dihydrolipoamide acetyltransferase K00627; Psort location: CytoplasmicMembrane, score: 9.82. (133 aa)
EKF05883.1CO2 hydration protein; KEGG: ppp:PHYPADRAFT_111923 0.54 hypothetical protein; K00970 poly(A) polymerase; Psort location: Cytoplasmic, score: 8.96. (439 aa)
EKF05885.1NAD(P)H-quinone oxidoreductase subunit M; KEGG: npu:Npun_F3688 1.8e-230 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
EKF05888.1KEGG: ava:Ava_0749 4.7e-296 NAD(P)H-quinone oxidoreductase subunit F K05577; Psort location: CytoplasmicMembrane, score: 10.00. (619 aa)
ndhHNAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (394 aa)
EKF05805.1Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (308 aa)
EKF05806.1KEGG: ana:alr2732 4.7e-42 coxA; cytochrome c oxidase subunit I; K02274 cytochrome c oxidase subunit I; Psort location: CytoplasmicMembrane, score: 9.82. (105 aa)
EKF05849.1Hypothetical protein; KEGG: sml:Smlt0161 0.64 sodC2; putative superoxide dismutase; K04565 Cu/Zn superoxide dismutase. (208 aa)
EKF05858.1KEGG: ana:alr2732 6.5e-235 coxA; cytochrome c oxidase subunit I; K02274 cytochrome c oxidase subunit I; Psort location: CytoplasmicMembrane, score: 10.00; Belongs to the heme-copper respiratory oxidase family. (457 aa)
EKF05859.1KEGG: npu:Npun_R3535 1.7e-92 cytochrome c oxidase, subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (200 aa)
EKF04686.1Putative nitrogen metabolic protein; KEGG: mgm:Mmc1_0977 1.4e-19 NAD-dependent epimerase/dehydratase; K00329 NADH dehydrogenase K00356; Psort location: Cytoplasmic, score: 8.96. (332 aa)
EKF04903.1Hypothetical protein; KEGG: pde:Pden_2307 0.0014 cytochrome c1; K00413 ubiquinol-cytochrome c reductase cytochrome c1 subunit. (201 aa)
EKF05194.1Hypothetical protein; KEGG: det:DET0729 5.0e-07 [Fe] hydrogenase, HymB subunit, putative; K00335 NADH dehydrogenase I subunit F. (216 aa)
EKF05314.1NAD-binding domain 4; KEGG: rha:RHA1_ro08518 2.8e-21 nucleoside-diphosphate-sugar epimerase K01798. (291 aa)
EKF05343.1Peptidase M16 inactive domain protein; KEGG: ana:alr5125 1.5e-180 processing protease; K01412 mitochondrial processing peptidase; Belongs to the peptidase M16 family. (427 aa)
EKF04498.1Cytochrome c oxidase subunit; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (298 aa)
EKF04499.1Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (558 aa)
EKF04500.1KEGG: ava:Ava_B0177 7.4e-108 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (239 aa)
EKF03810.1Hypothetical protein; KEGG: tel:tsr0706 1.1e-10 ndhL; NADH dehydrogenase subunit; K05583 NADH dehydrogenase I subunit L. (39 aa)
EKF03728.1NAD(P)H-quinone oxidoreductase subunit F; KEGG: npu:Npun_R6185 0. proton-translocating NADH-quinone oxidoreductase, chain L K05577; Psort location: CytoplasmicMembrane, score: 10.00. (699 aa)
ndhDProton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4 family. (524 aa)
EKF03486.1Hypothetical protein; KEGG: abc:ACICU_03555 0.34 ureidoglycolate hydrolase; K01483 ureidoglycolate hydrolase. (64 aa)
ndhD-2Proton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4 family. (562 aa)
EKF03253.1Fasciclin domain protein; KEGG: ctc:CTC02609 0.092 rpoB; DNA-directed RNA polymerase subunit beta K03043; Psort location: CytoplasmicMembrane, score: 9.82. (133 aa)
EKF03277.1Plastoquinol--plastocyanin reductase; KEGG: ana:all0606 2.3e-42 petC; cytochrome b6/F-complex iron-sulfur protein; K02636 cytochrome b6-f complex iron-sulfur subunit; Psort location: CytoplasmicMembrane, score: 9.82. (141 aa)
ndhCNADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (120 aa)
ndhKNADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (245 aa)
ndhJNADH dehydrogenase, subunit C; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (174 aa)
EKE98666.1KEGG: ava:Ava_0448 1.7e-85 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (195 aa)
EKE98668.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (560 aa)
EKE98669.1Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (325 aa)
EKE98764.1Oxidoreductase family, NAD-binding Rossmann fold protein; KEGG: npu:Npun_R3642 4.8e-26 oxidoreductase domain-containing protein. (97 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (317 aa)
EKE98778.1Cytochrome oxidase assembly protein; KEGG: tro:trd_A0395 4.9e-21 protoheme IX farnesyltransferase (heme O synthase) (HemeB farnesyltransferase) K02301; Psort location: CytoplasmicMembrane, score: 10.00. (340 aa)
EKE98779.1Cytochrome c oxidase subunit; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (365 aa)
EKE98780.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (578 aa)
EKE98781.1KEGG: ava:Ava_0530 7.3e-101 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (208 aa)
EKE98576.1Hypothetical protein; KEGG: ajs:Ajs_3012 0.010 lipopolysaccharide biosynthesis K08252; Psort location: Periplasmic, score: 9.83. (280 aa)
ndhOHypothetical protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (71 aa)
EKE98164.1RNA-binding protein; KEGG: pmj:P9211_11941 3.2e-20 rbpD; peptidylprolyl isomerase. (102 aa)
EKE97812.1Putative mucleoside-diphosphate-sugar epimerase; KEGG: mar:MAE_23570 1.3e-17 3-beta hydroxysteroid dehydrogenase/isomerase. (494 aa)
EKE97830.1Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (306 aa)
EKE97831.1Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (561 aa)
EKE97833.1KEGG: ava:Ava_3575 4.7e-106 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (222 aa)
EKE97463.1Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. (548 aa)
EKE97464.1H(+)-transporting two-sector protein; KEGG: ava:Ava_4653 1.4e-65 bidirectional hydrogenase complex protein HoxE K05586; Psort location: Cytoplasmic, score: 9.26. (181 aa)
petCTat pathway signal sequence; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. (179 aa)
EKF03214.1Plastoquinol--plastocyanin; KEGG: ana:all0606 2.2e-51 petC; cytochrome b6/F-complex iron-sulfur protein; K02636 cytochrome b6-f complex iron-sulfur subunit. (145 aa)
EKF02929.1NAD dependent epimerase/dehydratase family protein; KEGG: npu:Npun_F0086 9.2e-94 NmrA family protein; Psort location: Cytoplasmic, score: 8.96. (219 aa)
EKF02676.1KEGG: npu:Npun_R4998 0. peptidase M16 domain-containing protein K07263. (927 aa)
ndhNHypothetical protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (158 aa)
EKF02047.1Cytochrome c oxidase subunit; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (281 aa)
EKF02048.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (552 aa)
EKF02050.1KEGG: cyn:Cyan7425_3956 3.9e-86 cytochrome c oxidase subunit III; K02276 cytochrome c oxidase subunit III; Psort location: CytoplasmicMembrane, score: 10.00. (203 aa)
EKF02096.1KEGG: ana:alr0762 1.0e-117 hoxU; bidirectional hydrogenase complex protein HoxU; K05588 diaphorase subunit of the bidirectional hydrogenase; Psort location: Cytoplasmic, score: 9.97. (238 aa)
EKF01942.1Fasciclin domain protein; KEGG: ava:Ava_3135 1.7e-46 hypothetical protein. (576 aa)
EKF01467.1Putative thioredoxin; KEGG: pth:PTH_2011 6.8e-07 nuoF; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit; K00335 NADH dehydrogenase I subunit F; Psort location: Cytoplasmic, score: 8.96. (178 aa)
EKF01392.1Putative NmrA family transcriptional regulator; KEGG: gox:GOX0529 4.4e-12 putative oxidoreductase K00100; Psort location: Cytoplasmic, score: 8.96. (299 aa)
EKF01264.1KEGG: npu:Npun_R2847 1.7e-229 peptidase M16 domain-containing protein; Psort location: Cytoplasmic, score: 8.96. (509 aa)
EKF01265.1KEGG: npu:Npun_R2846 1.4e-216 peptidase M16 domain-containing protein. (509 aa)
EKF01164.1Hypothetical protein; KEGG: syg:sync_0549 4.1e-20 petB; cytochrome b6 K02635; Psort location: CytoplasmicMembrane, score: 10.00. (188 aa)
EKF01024.1NAD-dependent epimerase/dehydratase; KEGG: mar:MAE_23570 2.1e-23 3-beta hydroxysteroid dehydrogenase/isomerase; Psort location: Cytoplasmic, score: 8.96. (270 aa)
EKF00538.1Hypothetical protein; KEGG: sce:YIR019C 0.050 MUC1; GPI-anchored cell surface glycoprotein (flocculin) required for pseudohyphal formation, invasive growth, flocculation, and biofilms; transcriptionally regulated by the MAPK pathway (via Ste12p and Tec1p) and the cAMP pathway (via Flo8p) K01178. (276 aa)
EKF00710.1Hypothetical protein; KEGG: ava:Ava_2796 1.5e-61 NAD(P)H-quinone oxidoreductase subunit 4 K05575. (146 aa)
ndhD-3Proton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4 family. (537 aa)
EKF00324.1Hydrolase, alpha/beta fold family protein; KEGG: ava:Ava_4455 8.1e-102 alpha/beta hydrolase fold K01054. (280 aa)
EKF00356.1NAD(P)H-quinone oxidoreductase subunit F; KEGG: npu:Npun_R4290 2.9e-287 NdhF3 family NAD(P)H dehydrogenase K05577; Psort location: CytoplasmicMembrane, score: 10.00. (618 aa)
EKF00357.1NAD(P)H-quinone oxidoreductase subunit D4; KEGG: npu:Npun_R4289 6.0e-225 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
EKF00360.1CO2 hydration protein; KEGG: mcc:700251 0.32 PSMA3; proteasome (prosome, macropain) subunit, alpha type, 3; K02727 20S proteasome subunit alpha 7. (376 aa)
ndhBProton-translocating NADH-quinone oxidoreductase, chain; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (520 aa)
EKF00214.1Putative RNA-binding protein; KEGG: pmj:P9211_11941 1.1e-19 rbpD; peptidylprolyl isomerase. (103 aa)
ndhENADH dehydrogenase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (101 aa)
EKE99675.1NADH-ubiquinone/plastoquinone oxidoreductase chain 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I subunit 6 family. (216 aa)
ndhINADH-plastoquinone oxidoreductase, I subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (194 aa)
ndhANADH dehydrogenase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (372 aa)
EKE99495.1KEGG: npu:Npun_R4070 6.5e-180 peptidase M16 domain-containing protein; Psort location: Cytoplasmic, score: 8.96. (413 aa)
EKE99498.1KEGG: npu:Npun_R4069 1.8e-168 peptidase M16 domain-containing protein. (406 aa)
ndhMNADH dehydrogenase I subunit M; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (164 aa)
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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