ID A0A2A2J0F0_9PSED Unreviewed; 476 AA.
AC A0A2A2J0F0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN Name=ccoN {ECO:0000313|EMBL:PAV49661.1};
GN ORFNames=CK486_02545 {ECO:0000313|EMBL:PAV49661.1};
OS Pseudomonas sp. HAR-UPW-AIA-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1985301 {ECO:0000313|EMBL:PAV49661.1, ECO:0000313|Proteomes:UP000243299};
RN [1] {ECO:0000313|Proteomes:UP000243299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAR-UPW-AIA-41 {ECO:0000313|Proteomes:UP000243299};
RA Kumari P., Krishnamurthi S.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV49661.1}.
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DR EMBL; NSLB01000001; PAV49661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2J0F0; -.
DR OrthoDB; 9806838at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000243299; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000243299};
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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..476
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT BINDING 62
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 209
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 259
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 260
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 347
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 349
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 476 AA; 52673 MW; F7195E7C3ACE03D4 CRC64;
MSTATTQQTA YNYKVVRQFA IMTVIWGIVG MAVGVLIAAQ LVWPELNLGL PWTSFGRLRP
LHTNAVIFAF GGCALFATSY YTVQRTCQAR LFGGPLATFT FWGWQLVILL AAITLPLGIT
TSKEYAELEW PIDILITVVW VAYAIVFFGT VAKRQTSHIY VGNWFFGGFI LTVAILHLVN
NAELPVTALK SYSAYAGATD AMIQWWYGHN AVGFFLTAGF LGMMYYFVPK QAGRPVYSYR
LSIVHFWALI AVYIWAGPHH LHYTALPDWA QSLGMVMSLI LLAPSWGGMI NGMMTLSGAW
HKLRSDPILR FLVVSLAFYG MSTFEGPMMA IKTVNALSHY TDWTIGHVHA GALGWVAMVS
IGSLYHLIPK VFGREEMHST GLINTHFWLA TIGTVLYIAS MWVNGITQGL MWRAVNEDGT
LTYSFVEALE AGHYGYLVRM IGGAIFLAGM LVMAYNTWRT VSSATAEQVQ AAGQPA
//
