FIXN_AZOC5
ID FIXN_AZOC5 Reviewed; 551 AA.
AC P98056; A8HZ09;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cytochrome c oxidase subunit 1 homolog;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide I homolog;
GN Name=fixN; OrderedLocusNames=AZC_4523;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8282187; DOI=10.1111/j.1574-6968.1993.tb06571.x;
RA Mandon K., Kaminski P.A., Mougel C., Desnoues N., Elmerich C.;
RT "Role of the fixGHI region of Azorhizobium caulinodans in free-living and
RT symbiotic nitrogen fixation.";
RL FEMS Microbiol. Lett. 114:185-189(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8169204; DOI=10.1128/jb.176.9.2560-2568.1994;
RA Mandon K., Kaminski P.A., Elmerich C.;
RT "Functional analysis of the fixNOQP region of Azorhizobium caulinodans.";
RL J. Bacteriol. 176:2560-2568(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. Co I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c or a
CC quinol are transferred to the bimetallic center formed by a high-spin
CC heme and copper B.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:D9IA43};
CC Note=Binds 1 copper ion per subunit, denoted as copper B.
CC {ECO:0000250|UniProtKB:D9IA43};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:D9IA43};
CC Note=Binds 2 heme b groups per subunit, denoted as high- and low-spin.
CC {ECO:0000250|UniProtKB:D9IA43};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74410; CAA52429.1; -; Genomic_DNA.
DR EMBL; AP009384; BAF90521.1; -; Genomic_DNA.
DR PIR; A55582; A55582.
DR RefSeq; WP_012173042.1; NC_009937.1.
DR AlphaFoldDB; P98056; -.
DR SMR; P98056; -.
DR STRING; 438753.AZC_4523; -.
DR EnsemblBacteria; BAF90521; BAF90521; AZC_4523.
DR KEGG; azc:AZC_4523; -.
DR eggNOG; COG3278; Bacteria.
DR HOGENOM; CLU_017702_3_4_5; -.
DR OMA; WGWQLII; -.
DR OrthoDB; 665754at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000000270; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045278; C:plasma membrane respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01661; cbb3_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR PANTHER; PTHR10422:SF29; PTHR10422:SF29; 1.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR00780; ccoN; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Respiratory chain; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..551
FT /note="Cytochrome c oxidase subunit 1 homolog"
FT /id="PRO_0000183468"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 132
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 281
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 332
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 419
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2; high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 421
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
SQ SEQUENCE 551 AA; 61843 MW; 0466F71CD04BFC4D CRC64;
MSIVQTPAKR MTGGELGLIL VFAALGFFSI VVAAKAYTPE YAFHAYLFAA ASIATVFVIG
NRYMDRPAEL PPQTIDGKPN YNMAPVKVGT LLAVFWGIAG FLIGVIIALQ MAYPLFNFDL
PWISFGRLRP LHTSAVIFAF GGNVLIATSF YVVQRTSHAR LAGYLAPWFV VLGYNFFIVI
AGTGYLLGIT QGKEYAEPEW YADLWLTIVW VTYFLVFLGT VLKRKEPHIY VANWFYLAFI
LTIAVLHLGN NAAIPVSVFS PKSYIVWSGV QDAMVQWWYG HNAVGFFLTA GFLALMYYFI
PKRADKPVYS YRLSIVHFWA LIFLYIWAGP HHLHYTALPD WAQTLGMTFS IMLWMPSWGG
MINGLMTLSG AWDKLRTDPI IRMMVVAVAF YGMATFEGPM MSVKSVNSLS HYTEWGIGHV
HSGALGWVAY ISFGAIYCLI PWLWNKREMY SMKAIEWHFW VSTLGIVLYI CAMWVAGILQ
GLMWRAYTAL GFLEYSFIET VEAMHPLYVI RAIGGILFLA GSLIMAWNVF MTITRAETVS
QPSGAALAPA E
