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AFZ55663.1 AFZ55663.1 AFZ55664.1 AFZ55664.1 AFZ55692.1 AFZ55692.1 AFZ55693.1 AFZ55693.1 AFZ55694.1 AFZ55694.1 AFZ56008.1 AFZ56008.1 AFZ56085.1 AFZ56085.1 AFZ56086.1 AFZ56086.1 ndhA ndhA ndhI ndhI AFZ56108.1 AFZ56108.1 ndhE ndhE atpC atpC atpD atpD ndhH ndhH ndhM ndhM ppa ppa atpB atpB atpE atpE atpG atpG atpF atpF atpH atpH atpA atpA atpG-2 atpG-2 ndhJ ndhJ ndhK ndhK ndhC ndhC AFZ57561.1 AFZ57561.1 AFZ57701.1 AFZ57701.1 ppk ppk AFZ58104.1 AFZ58104.1 AFZ58213.1 AFZ58213.1 ndhD ndhD ndhN ndhN ndhD-2 ndhD-2 ndhD-3 ndhD-3 AFZ59535.1 AFZ59535.1 AFZ59619.1 AFZ59619.1 AFZ59620.1 AFZ59620.1 AFZ59621.1 AFZ59621.1 AFZ59879.1 AFZ59879.1 AFZ59881.1 AFZ59881.1 ctaB ctaB AFZ60144.1 AFZ60144.1 AFZ60145.1 AFZ60145.1 AFZ60146.1 AFZ60146.1 AFZ60147.1 AFZ60147.1 ndhB ndhB AFZ60728.1 AFZ60728.1 AFZ60729.1 AFZ60729.1 AFZ60730.1 AFZ60730.1
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AFZ55663.1PFAM: Bacterial Cytochrome Ubiquinol Oxidase; COGs: COG1271 Cytochrome bd-type quinol oxidase subunit 1; InterPro IPR002585; KEGG: naz:Aazo_2590 cytochrome bd ubiquinol oxidase subunit I; PFAM: Cytochrome d ubiquinol oxidase, subunit I; SPTR: Cytochrome bd ubiquinol oxidase subunit I. (481 aa)
AFZ55664.1PFAM: Cytochrome oxidase subunit II; TIGRFAM: cytochrome d oxidase, subunit II (cydB); COGs: COG1294 Cytochrome bd-type quinol oxidase subunit 2; InterPro IPR003317; KEGG: naz:Aazo_2591 cytochrome d ubiquinol oxidase subunit II; PFAM: Cytochrome d ubiquinol oxidase, subunit II; SPTR: Cytochrome d ubiquinol oxidase, subunit II; TIGRFAM: Cytochrome d ubiquinol oxidase, subunit II. (337 aa)
AFZ55692.1Cytochrome 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). (314 aa)
AFZ55693.1Cytochrome 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. (548 aa)
AFZ55694.1PFAM: Cytochrome c oxidase subunit III; COGs: COG1845 Heme/copper-type cytochrome/quinol oxidase subunit 3; InterPro IPR000298; KEGG: naz:Aazo_2639 cytochrome c oxidase; PFAM: Cytochrome c oxidase, subunit III; PRIAM: Cytochrome-c oxidase; SPTR: Cytochrome-c oxidase. (198 aa)
AFZ56008.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; COGs: COG0479 Succinate dehydrogenase/fumarate reductase Fe-S protein subunit; InterPro IPR004489; KEGG: naz:Aazo_0058 succinate dehydrogenase and fumarate reductase iron-sulfur protein; PRIAM: Succinate dehydrogenase; SPTR: Succinate dehydrogenase and fumarate reductase iron-sulfur protein; TIGRFAM: Succinate dehydrogenase/fumarate reductase iron-sulphur protein. (332 aa)
AFZ56085.1NAD(P)H dehydrogenase, subunit NdhF3 family; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: NAD(P)H dehydrogenase, subunit NdhF3 family; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterPro IPR001516:IPR001750:IPR010217; KEGG: naz:Aazo_1866 NAD(P)H dehydrogenase subunit NdhF3 family; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal; PRIAM: NADH dehydrogenase (quinone); SPTR: [...] (618 aa)
AFZ56086.1PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR001750:IPR010227; KEGG: naz:Aazo_1867 proton-translocating NADH-quinone oxidoreductase subunit M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; PRIAM: NADH dehydrogenase (quinone); SPTR: Proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: NADH-quinone oxidoreductase, chain M/4. (500 aa)
ndhANADH dehydrogenase 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. (372 aa)
ndhINAD(P)H-quinone oxidoreductase subunit I; 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)
AFZ56108.1NADH dehydrogenase subunit J; 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. (203 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)
atpCATP synthase F1 subcomplex epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (164 aa)
atpDATP synthase F1 subcomplex beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (482 aa)
ndhHNADH dehydrogenase subunit D; 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)
ndhMNAD(P)H-quinone oxidoreductase 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. (114 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (170 aa)
atpBATP synthase F0 subcomplex A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (252 aa)
atpEATP synthase F0 subcomplex C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (81 aa)
atpGATP synthase F0 subcomplex B' subunit; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. Belongs to the ATPase B chain family. (163 aa)
atpFATP synthase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (183 aa)
atpHATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (184 aa)
atpAATP synthase F1 subcomplex alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (506 aa)
atpG-2ATP synthase F1 subcomplex gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (315 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. (175 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. (244 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)
AFZ57561.1NADH dehydrogenase (ubiquinone); PFAM: Pyridine nucleotide-disulphide oxidoreductase; COGs: COG1252 NADH dehydrogenase FAD-containing subunit; InterPro IPR013027; KEGG: ana:all1127 NADH dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; PRIAM: NADH dehydrogenase (ubiquinone); SPTR: NADH dehydrogenase. (452 aa)
AFZ57701.1NADH dehydrogenase (ubiquinone); PFAM: Pyridine nucleotide-disulphide oxidoreductase; COGs: COG1252 NADH dehydrogenase FAD-containing subunit; InterPro IPR013027; KEGG: naz:Aazo_5049 FAD-dependent pyridine nucleotide-disulfide oxidoreductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; PRIAM: NADH dehydrogenase (ubiquinone); SPTR: FAD-dependent pyridine nucleotide-disulfide oxidoreductase. (453 aa)
ppkPolyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (721 aa)
AFZ58104.1Succinate dehydrogenase subunit A; PFAM: domain; FAD binding domain; TIGRFAM: L-aspartate oxidase; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; COGs: COG1053 Succinate dehydrogenase/fumarate reductase flavoprotein subunit; InterPro IPR014006:IPR003953:IPR004112; KEGG: naz:Aazo_1206 succinate dehydrogenase or fumarate reductase flavoprotein subunit; PFAM: Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal; Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal; PRIAM: Succinate dehydrogenase (ubiqu [...] (575 aa)
AFZ58213.1PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5 C-terminus; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterPro IPR003945:IPR001516:IPR001750; KEGG: naz:Aazo_0150 proton-translocating NADH-quinone oxidoreductase subunit L; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-term [...] (693 aa)
ndhDNADH dehydrogenase subunit 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)
ndhNNAD(P)H-quinone oxidoreductase subunit N; 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)
ndhD-2NADH dehydrogenase subunit 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. (555 aa)
ndhD-3NADH dehydrogenase subunit 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. (534 aa)
AFZ59535.1Succinate dehydrogenase subunit C; PFAM: Cysteine-rich domain; COGs: COG2048 Heterodisulfide reductase subunit B; InterPro IPR004017; KEGG: npu:Npun_F4560 hypothetical protein; PFAM: Cysteine-rich domain; PRIAM: CoB--CoM heterodisulfide reductase; SPTR: Putative uncharacterized protein. (301 aa)
AFZ59619.1NAD(P)-dependent nickel-iron dehydrogenase diaphorase component subunit HoxU; PFAM: 2Fe-2S iron-sulfur cluster binding domain; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; 4Fe-4S binding domain; COGs: COG1034 NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G); InterPro IPR019574:IPR001041:IPR001450; KEGG: ava:Ava_4657 bidirectional hydrogenase complex protein HoxU; PFAM: NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding; Ferredoxin; 4Fe-4S binding domain; SMART: NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding; SPTR: 4 [...] (238 aa)
AFZ59620.1NAD(P)-dependent nickel-iron dehydrogenase flavin-containing subunit; PFAM: NADH-ubiquinone oxidoreductase-F iron-sulfur binding region; Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit; SLBB domain; COGs: COG1894 NADH:ubiquinone oxidoreductase NADH-binding (51 kD) subunit; InterPro IPR019575:IPR011538:IPR019554; KEGG: ana:alr0752 hydrogenase subunit; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; PRIAM: NADH dehydrogenase (quinone) [...] (533 aa)
AFZ59621.1NAD(P)-dependent nickel-iron dehydrogenase diaphorase component subunit HoxE; PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; COGs: COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit; InterPro IPR002023; KEGG: ava:Ava_4653 bidirectional hydrogenase complex protein HoxE; PFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit; SPTR: NAD(P)-dependent nickel-iron dehydrogenase diaphorase component subunit HoxE. (171 aa)
AFZ59879.1NAD(P)H dehydrogenase, subunit NdhF3 family; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: NAD(P)H dehydrogenase, subunit NdhF3 family; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterPro IPR001750:IPR010217; KEGG: naz:Aazo_4078 NAD(P)H dehydrogenase subunit NdhF3 family; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; PRIAM: NADH dehydrogenase (quinone); SPTR: NAD(P)H dehydrogenase, subunit NdhF3 family; TIGRFAM: NAD(P)H deh [...] (619 aa)
AFZ59881.1PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR001750:IPR010227; KEGG: naz:Aazo_4080 proton-translocating NADH-quinone oxidoreductase subunit M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; PRIAM: NADH dehydrogenase (quinone); SPTR: Proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: NADH-quinone oxidoreductase, chain M/4. (500 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. (314 aa)
AFZ60144.1PFAM: Cytochrome oxidase assembly protein; COGs: COG1612 Uncharacterized protein required for cytochrome oxidase assembly; InterPro IPR003780; KEGG: naz:Aazo_3572 cytochrome oxidase assembly; PFAM: Heme A synthase/Protoheme IX farnesyltransferase; SPTR: Cytochrome oxidase assembly. (307 aa)
AFZ60145.1Cytochrome 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). (340 aa)
AFZ60146.1Cytochrome 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. (564 aa)
AFZ60147.1PFAM: Cytochrome c oxidase subunit III; COGs: COG1845 Heme/copper-type cytochrome/quinol oxidase subunit 3; InterPro IPR000298; KEGG: naz:Aazo_3575 cytochrome c oxidase; PFAM: Cytochrome c oxidase, subunit III; PRIAM: Cytochrome-c oxidase; SPTR: Cytochrome-c oxidase. (206 aa)
ndhBNADH dehydrogenase subunit N; 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. (518 aa)
AFZ60728.1PFAM: Cytochrome c oxidase subunit III; COGs: COG1845 Heme/copper-type cytochrome/quinol oxidase subunit 3; InterPro IPR000298; KEGG: naz:Aazo_3658 cytochrome c oxidase subunit III; PFAM: Cytochrome c oxidase, subunit III; PRIAM: Cytochrome-c oxidase; SPTR: Cytochrome c oxidase subunit III. (200 aa)
AFZ60729.1Cytochrome 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)
AFZ60730.1Cytochrome 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). (308 aa)
Your Current Organism:
Anabaena cylindrica
NCBI taxonomy Id: 272123
Other names: A. cylindrica PCC 7122, Anabaena cylindrica IAM M-1, Anabaena cylindrica NIES-19, Anabaena cylindrica PCC 7122, Anabaena cylindrica UTEX B 629, Anabaena sp. ATCC 27899, Anabaena sp. PCC 7122
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