CYDA_AZOVI
ID CYDA_AZOVI Reviewed; 537 AA.
AC Q09049;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cytochrome bd ubiquinol oxidase subunit 1;
DE EC=7.1.1.7 {ECO:0000250|UniProtKB:P0ABJ9};
DE AltName: Full=Cytochrome d ubiquinol oxidase subunit I;
GN Name=cydA;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA;
RX PubMed=1655703; DOI=10.1128/jb.173.19.6230-6241.1991;
RA Moshiri F., Chawla A., Maier R.J.;
RT "Cloning, characterization, and expression in Escherichia coli of the genes
RT encoding the cytochrome d oxidase complex from Azotobacter vinelandii.";
RL J. Bacteriol. 173:6230-6241(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA;
RX PubMed=1660468; DOI=10.1016/s0021-9258(18)54479-3;
RA Moshiri F., Smith E.G., Taormino J.P., Maier R.J.;
RT "Transcriptional regulation of cytochrome d in nitrogen-fixing Azotobacter
RT vinelandii. Evidence that up-regulation during N2 fixation is independent
RT of nifA but dependent on ntrA.";
RL J. Biol. Chem. 266:23169-23174(1991).
RN [3]
RP FUNCTION.
RX PubMed=2170336; DOI=10.1128/jb.172.10.6010-6019.1990;
RA Kelly M.J.S., Poole R.K., Yates M.G., Kennedy C.;
RT "Cloning and mutagenesis of genes encoding the cytochrome bd terminal
RT oxidase complex in Azotobacter vinelandii: mutants deficient in the
RT cytochrome d complex are unable to fix nitrogen in air.";
RL J. Bacteriol. 172:6010-6019(1990).
CC -!- FUNCTION: May be involved in maintaining the low intracellular oxygen
CC concentration required for nitrogen fixation.
CC {ECO:0000269|PubMed:1655703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4
CC H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC Note=Binds 1 protoheme IX center (heme b558) per subunit.
CC {ECO:0000250|UniProtKB:P0ABJ9};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC Note=Binds 1 protoheme IX center (heme b595) per heterodimer, in
CC conjunction with CydB. {ECO:0000250|UniProtKB:P0ABJ9};
CC -!- COFACTOR:
CC Name=heme d cis-diol; Xref=ChEBI:CHEBI:62814;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC Note=Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in
CC conjunction with CydB. {ECO:0000250|UniProtKB:P0ABJ9};
CC -!- SUBUNIT: Heterodimer of subunits I and II.
CC {ECO:0000250|UniProtKB:P0ABJ9}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000305}.
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DR EMBL; M77787; AAA22123.1; -; Genomic_DNA.
DR EMBL; S57066; AAB19986.1; -; Genomic_DNA.
DR PIR; A38170; A38170.
DR AlphaFoldDB; Q09049; -.
DR SMR; Q09049; -.
DR GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365; PTHR30365; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..537
FT /note="Cytochrome bd ubiquinol oxidase subunit 1"
FT /id="PRO_0000183917"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..96
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..189
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..394
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..537
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b595"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 188
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b558"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b558"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 537 AA; 59719 MW; 8F78A49F6AB4902E CRC64;
MISESVVDLS RLQFAMTALY HFLFVPLTLG MTFLLAIMES VYVMTGKQVY KDMVKFWGKL
FGINFALGVT TGITMEFQFG TNWAYYSHYV GDIFGAPLAI EGLTAFFLES TFIGMFFFGW
DRLSKIQHLA VTWLVALGSN LSALWILVAN GWMQHPVGAE FNFETMRMEL VDFGALLLNP
VAQVKFVHTV ASGYVTGAVF VLAISSYYLL KKRDLGFARR SFAIASAFGM ASILSVIVLG
DESGYEVGEV QKAKLAAIEA EWETHPAPAS FTLIGFPNEE EQRTDFAVKI PWVLGIIATR
SLDEQVIGIK DLIADHEARI RNGMVRYGLL EELRAGNKSP EKIAAFNEVK DDLGYGLLLK
KYTPNVVDAS EEQIKQAAKD TIPSVASMFW SFRAMVGAGF AMLILFVCAF WASARKNEES
KPWLLKFALY SLPLPWIATQ TGWFVAEHGR QPWTIGGVLP THLSASSLST GDLWGSLIAL
IAFYTLLLVV EMYLMIRFAR LGPSSLHTGR YHFEQLEQHA VKHASPSQAD PQQPVNA
