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qoxD qoxD qoxC qoxC qoxB qoxB qoxA qoxA CHR53_17775 CHR53_17775 CHR53_17780 CHR53_17780 CHR53_18280 CHR53_18280 CHR53_18535 CHR53_18535 CHR53_18540 CHR53_18540 CHR53_18555 CHR53_18555 CHR53_18565 CHR53_18565 CHR53_18570 CHR53_18570 CHR53_18575 CHR53_18575 CHR53_18580 CHR53_18580 CHR53_18780 CHR53_18780 CHR53_18785 CHR53_18785 CHR53_18790 CHR53_18790 CHR53_19750 CHR53_19750 CHR53_21760 CHR53_21760 CHR53_23325 CHR53_23325 CHR53_23330 CHR53_23330 CHR53_23335 CHR53_23335 CHR53_23400 CHR53_23400 CHR53_23690 CHR53_23690 nuoN nuoN CHR53_26970 CHR53_26970 CHR53_26975 CHR53_26975 nuoK nuoK CHR53_26985 CHR53_26985 nuoI nuoI nuoH nuoH nuoD nuoD CHR53_27005 CHR53_27005 nuoB nuoB nuoA nuoA CHR53_27745 CHR53_27745 CHR53_27855 CHR53_27855 CHR53_00105 CHR53_00105 CHR53_00110 CHR53_00110 CHR53_02260 CHR53_02260 ctaB ctaB CHR53_03620 CHR53_03620 CHR53_03625 CHR53_03625 GCA_001636315_03544 GCA_001636315_03544 CHR53_05085 CHR53_05085 CHR53_05090 CHR53_05090 CHR53_05095 CHR53_05095 CHR53_05100 CHR53_05100 CHR53_05105 CHR53_05105 CHR53_05110 CHR53_05110 CHR53_05115 CHR53_05115 CHR53_05120 CHR53_05120 GCA_001636315_03553 GCA_001636315_03553 CHR53_05125 CHR53_05125 CHR53_05645 CHR53_05645 CHR53_06035 CHR53_06035 CHR53_06400 CHR53_06400 CHR53_06405 CHR53_06405 CHR53_06410 CHR53_06410 CHR53_06415 CHR53_06415 CHR53_06420 CHR53_06420 GCA_001636315_03818 GCA_001636315_03818 CHR53_06430 CHR53_06430 CHR53_06435 CHR53_06435 CHR53_06440 CHR53_06440 CHR53_06445 CHR53_06445 CHR53_06450 CHR53_06450 CHR53_06455 CHR53_06455 CHR53_08515 CHR53_08515 ctaA ctaA ctaB-2 ctaB-2 coxB coxB ctaD ctaD CHR53_09045 CHR53_09045 ctaF ctaF ctaG ctaG CHR53_09060 CHR53_09060 acpP acpP CHR53_09845 CHR53_09845 CHR53_09850 CHR53_09850 fabG-2 fabG-2 CHR53_10475 CHR53_10475 CHR53_12495 CHR53_12495 CHR53_12500 CHR53_12500 CHR53_12505 CHR53_12505 CHR53_12510 CHR53_12510 CHR53_12515 CHR53_12515 CHR53_14855 CHR53_14855 CHR53_14880 CHR53_14880 CHR53_15905 CHR53_15905
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
qoxDUnannotated protein. (93 aa)
qoxCUnannotated protein. (198 aa)
qoxBUnannotated protein; Belongs to the heme-copper respiratory oxidase family. (648 aa)
qoxAUnannotated protein; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. (301 aa)
CHR53_17775Unannotated protein. (178 aa)
CHR53_17780Unannotated protein. (488 aa)
CHR53_18280Unannotated protein. (199 aa)
CHR53_18535Unannotated protein. (158 aa)
CHR53_18540Unannotated protein; Belongs to the heme-copper respiratory oxidase family. (552 aa)
CHR53_18555Unannotated protein. (78 aa)
CHR53_18565Unannotated protein. (230 aa)
CHR53_18570Unannotated protein. (77 aa)
CHR53_18575Unannotated protein. (69 aa)
CHR53_18580Unannotated protein. (414 aa)
CHR53_18780Unannotated protein; Component of the menaquinol-cytochrome c reductase complex. (256 aa)
CHR53_18785Unannotated protein. (224 aa)
CHR53_18790Unannotated protein. (168 aa)
CHR53_19750Unannotated protein. (362 aa)
CHR53_21760Unannotated protein. (190 aa)
CHR53_23325Unannotated protein. (341 aa)
CHR53_23330Unannotated protein. (452 aa)
CHR53_23335Unannotated protein. (299 aa)
CHR53_23400Unannotated protein. (111 aa)
CHR53_23690Unannotated protein. (128 aa)
nuoNUnannotated protein; NDH-1 shuttles electrons from NADH, 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 a menaquinone. 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 2 family. (504 aa)
CHR53_26970Unannotated protein. (502 aa)
CHR53_26975Unannotated protein. (621 aa)
nuoKUnannotated protein; NDH-1 shuttles electrons from NADH, 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 a menaquinone. 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 4L family. (104 aa)
CHR53_26985Unannotated protein; 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. (172 aa)
nuoIUnannotated protein; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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. (141 aa)
nuoHUnannotated protein; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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. This subunit may bind ubiquinone. (334 aa)
nuoDUnannotated protein; NDH-1 shuttles electrons from NADH, 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 a menaquinone. 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 49 kDa subunit family. (366 aa)
CHR53_27005Unannotated protein. (431 aa)
nuoBUnannotated protein; NDH-1 shuttles electrons from NADH, 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 a menaquinone. 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. (170 aa)
nuoAUnannotated protein; NDH-1 shuttles electrons from NADH, 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 a menaquinone. 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 3 family. (124 aa)
CHR53_27745Unannotated protein. (760 aa)
CHR53_27855Unannotated protein. (134 aa)
CHR53_00105Unannotated protein. (231 aa)
CHR53_00110Unannotated protein. (221 aa)
CHR53_02260Unannotated protein. (322 aa)
ctaBUnannotated protein; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (342 aa)
CHR53_03620Unannotated protein. (191 aa)
CHR53_03625Unannotated protein. (255 aa)
GCA_001636315_03544Unannotated protein. (44 aa)
CHR53_05085Unannotated protein. (189 aa)
CHR53_05090Unannotated protein. (226 aa)
CHR53_05095Unannotated protein. (945 aa)
CHR53_05100Unannotated protein. (112 aa)
CHR53_05105Unannotated protein. (494 aa)
CHR53_05110Unannotated protein. (158 aa)
CHR53_05115Unannotated protein. (110 aa)
CHR53_05120Unannotated protein. (120 aa)
GCA_001636315_03553Unannotated protein. (88 aa)
CHR53_05125Unannotated protein. (140 aa)
CHR53_05645Unannotated protein. (314 aa)
CHR53_06035Unannotated protein. (509 aa)
CHR53_06400Unannotated protein. (389 aa)
CHR53_06405Unannotated protein. (543 aa)
CHR53_06410Unannotated protein; Belongs to the UPF0753 family. (872 aa)
CHR53_06415Unannotated protein. (123 aa)
CHR53_06420Unannotated protein. (163 aa)
GCA_001636315_03818Unannotated protein. (48 aa)
CHR53_06430Unannotated protein. (153 aa)
CHR53_06435Unannotated protein. (559 aa)
CHR53_06440Unannotated protein. (211 aa)
CHR53_06445Unannotated protein. (185 aa)
CHR53_06450Unannotated protein. (234 aa)
CHR53_06455Unannotated protein. (245 aa)
CHR53_08515Unannotated protein. (120 aa)
ctaAUnannotated protein; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 1 subfamily. (301 aa)
ctaB-2Unannotated protein; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (308 aa)
coxBUnannotated protein; 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). (384 aa)
ctaDUnannotated protein; 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. (622 aa)
CHR53_09045Unannotated protein. (209 aa)
ctaFUnannotated protein. (111 aa)
ctaGUnannotated protein. (300 aa)
CHR53_09060Unannotated protein. (154 aa)
acpPUnannotated protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. (77 aa)
CHR53_09845Unannotated protein. (426 aa)
CHR53_09850Unannotated protein. (429 aa)
fabG-2Unannotated protein. (240 aa)
CHR53_10475Unannotated protein. (159 aa)
CHR53_12495Unannotated protein. (204 aa)
CHR53_12500Unannotated protein; Belongs to the sigma-70 factor family. ECF subfamily. (181 aa)
CHR53_12505Unannotated protein. (214 aa)
CHR53_12510Unannotated protein. (131 aa)
CHR53_12515Unannotated protein. (170 aa)
CHR53_14855Unannotated protein. (389 aa)
CHR53_14880Unannotated protein. (150 aa)
CHR53_15905Unannotated protein. (64 aa)
Your Current Organism:
Bacillus mesonae
NCBI taxonomy Id: 1193713
Other names: B. mesonae, Bacillus mesonae Liu et al. 2014, Bacillus sp. FJAT-13985, CGMCC1.12238, DSM 25968, strain FJAT-13985
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