FIXN_AGRT7
ID FIXN_AGRT7 Reviewed; 539 AA.
AC P98055;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
OS Agrobacterium tumefaciens (strain T37).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7753030; DOI=10.1007/bf00705651;
RA Schlueter A., Rueberg S., Kraemer M., Weidner S., Priefer U.;
RT "A homolog of the Rhizobium meliloti nitrogen fixation gene fixN is
RT involved in the production of a microaerobically induced oxidase activity
RT in the phytopathogenic bacterium Agrobacterium tumefaciens.";
RL Mol. Gen. Genet. 247:206-215(1995).
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}.
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DR EMBL; Z46239; CAA86308.1; -; Genomic_DNA.
DR PIR; S54758; S49495.
DR AlphaFoldDB; P98055; -.
DR SMR; P98055; -.
DR UniPathway; UPA00705; -.
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; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..539
FT /note="Cytochrome c oxidase subunit 1 homolog"
FT /id="PRO_0000183467"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 117
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 266
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 316
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 317
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 404
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 406
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 539 AA; 60651 MW; 6D99827DCA2E0C5F CRC64;
MNYTLETADR ALGAFPALLG AAFAHDSLFA AHMWVLFFTL VVSTLLLLRR VSFLPPVAGP
PCRRTEYFDE VVKYGVMATV FWGVVGFLVG VVVALQLAFP DLNIAPYFNF GRMRPLHTSA
VIFAFGGNAL IATSFYVVQR TCRARLFGGN LGWFVFWGYN LFIIMAATGY LLGITQGREY
AEPEWYVDLW LTIVWVAYLA TFLGTILTRK EPHISVANWF YLSFIVTIAM LHIVNNLAVP
VSFLGVKSYS AFSGVQAALT QWWYGHNAVG FFLTAGFLGM MYYFIPKQVN RPVYSYRLSI
IHFWALIFMY IWAGPHHLHY TALPDWAQTL GMVFSIMLWM PSWGGMINGL MTLSGAWDKI
RTDPIVRMMV MAVAFYGMAT FEGPMMSIKA VNSLSHYTDW TIGHVHSGAL GWNGMITFGA
IYYLTPKLWG RDRLYSLQLV NWHFWLATLG IVVYAAVMWV AGIQQALMWR EYDSQGFLVY
SFAESVAALF PYYVMRALGG LMFLSGALIM AYNVTMTILG HQREEGASKG AAPSLQPAE
