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Database: UniProt
Entry: I7GZQ4_9HELI
LinkDB: I7GZQ4_9HELI
Original site: I7GZQ4_9HELI 
ID   I7GZQ4_9HELI            Unreviewed;       487 AA.
AC   I7GZQ4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Cb-type cytochrome C oxidase subunit I {ECO:0000313|EMBL:BAM33451.1};
DE   SubName: Full=Cytochrome c oxidase, cbb3-type, subunit I {ECO:0000313|EMBL:EFR46090.1};
DE            EC=1.9.3.1 {ECO:0000313|EMBL:BAM33451.1, ECO:0000313|EMBL:EFR46090.1};
GN   Name=fixN {ECO:0000313|EMBL:BAM33451.1};
GN   Synonyms=ccoN {ECO:0000313|EMBL:EFR46090.1};
GN   ORFNames=HCBAA847_2236 {ECO:0000313|EMBL:BAM33451.1}, HCCG_00636
GN   {ECO:0000313|EMBL:EFR46090.1};
OS   Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM33451.1, ECO:0000313|Proteomes:UP000006036};
RN   [1] {ECO:0000313|EMBL:EFR46090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 18818 {ECO:0000313|EMBL:EFR46090.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA   Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA   Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Helicobacter cinaedi strain CCUG 18818.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAM33451.1, ECO:0000313|Proteomes:UP000006036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM33451.1,
RC   ECO:0000313|Proteomes:UP000006036};
RX   PubMed=23012276; DOI=10.1128/JB.01347-12;
RA   Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT   "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT   BAA-847.";
RL   J. Bacteriol. 194:5692-5692(2012).
RN   [3] {ECO:0000313|EMBL:BAM33451.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM33451.1};
RA   Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000005755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 18818 {ECO:0000313|Proteomes:UP000005755};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species isolated
RT   from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-e00814(2014).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC       Note=Binds 1 copper ion per subunit, denoted as copper B.
CC       {ECO:0000256|PIRSR:PIRSR604677-50};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC       Note=Binds 2 heme groups per subunit, denoted as high- and low-spin.
CC       {ECO:0000256|PIRSR:PIRSR604677-50};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000370}.
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DR   EMBL; AP012492; BAM33451.1; -; Genomic_DNA.
DR   EMBL; DS990391; EFR46090.1; -; Genomic_DNA.
DR   RefSeq; WP_002955939.1; NZ_DS990391.1.
DR   AlphaFoldDB; I7GZQ4; -.
DR   KEGG; hcb:HCBAA847_2236; -.
DR   PATRIC; fig|1206745.3.peg.2360; -.
DR   eggNOG; COG3278; Bacteria.
DR   HOGENOM; CLU_017702_3_4_7; -.
DR   OrthoDB; 9806838at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000005755; Unassembled WGS sequence.
DR   Proteomes; UP000006036; Chromosome 1.
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   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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   NCBIfam; TIGR00780; ccoN; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF29; CYTOCHROME C OXIDASE SUBUNIT 1 HOMOLOG, BACTEROID; 1.
DR   Pfam; PF00115; COX1; 1.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|PIRSR:PIRSR604677-50, ECO:0000256|RuleBase:RU000370};
KW   Iron {ECO:0000256|PIRSR:PIRSR604677-50};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604677-50};
KW   Oxidoreductase {ECO:0000313|EMBL:BAM33451.1};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000370};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000370}.
FT   TRANSMEM        12..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..487
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   BINDING         60
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:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         218
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         268
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         269
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         356
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:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         358
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:0000256|PIRSR:PIRSR604677-50"
SQ   SEQUENCE   487 AA;  55470 MW;  3F85769FC1EB3EF1 CRC64;
     MQTNTLEYDY SIAKLFVFSA MAFGFVGLLI GVVIAFQMAF PDLNYLASEY GTFGRLRPLH
     TNGIIYGFTL SGIWASWYYL GQRVLKITYK EHPFLRTVGL AHFWIYIVLM ALAVISLFAG
     LTQSKEYSEL IWPLDIIVVV VWVLWGVSLF GSMGVRREQT IYISLWYFIA TFVGISALYI
     FNNLAIPTYF VAGVGSVLHS ISFYAGTNDA MVQWWWGHNA VAFVFTSGII GLIYYFLPKE
     SGQPIFSYKL TLFSFWGLMF IYIWAGGHHL IYSTTPDWIQ TLGSVFSVIL ILPSWGTAIN
     MLLTMRGQWH QIKESPMIKF LILASTWYML TTLEGPIQSI RSVNGLAHFT DWIIGHVHDA
     ALGWVGFMVI AACFHMVPRI FKREIYSKKL MDAQFWIMTT GIILYFSSMW IAGITQGMMW
     RDVDENGSLV YSFIDTVTAL FPYYLIRAIG GLMYLIGFIM FIYNIMMTIS SGRVLDKEPQ
     NATPMAA
//
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