ID A0A2A8HY02_9SPHN Unreviewed; 549 AA.
AC A0A2A8HY02;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN ORFNames=B2G71_05795 {ECO:0000313|EMBL:PEQ13822.1};
OS Novosphingobium sp. PC22D.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ13822.1, ECO:0000313|Proteomes:UP000220675};
RN [1] {ECO:0000313|EMBL:PEQ13822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC22D {ECO:0000313|EMBL:PEQ13822.1};
RA Peterson S.W.;
RL Submitted (FEB-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:PEQ13822.1}.
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DR EMBL; MWMO01000002; PEQ13822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8HY02; -.
DR OrthoDB; 9806838at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000220675; 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:UP000220675};
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 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..549
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT BINDING 120
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 269
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 319
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 320
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 407
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 409
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 549 AA; 61595 MW; C1436391073537DD CRC64;
MQTVLARAGI WLVVLLFAVI AVAAAADGGF AIHMSIVALA ALIGLWVSIS GADYAGIARG
ILKIPDEGRY DDDPVRWGVI ATVFWGIAGF LAGLFIALQL TWPVLNLEPF LNFGRLRPLH
TSAVIFAFGG NALIATSFYV VQRTCRARLA FPGLARFVFW GYQLFIVLAA TGYLLGVTQS
KEYAEPEWYV DWWLTIVWVA YLVVFAGTIL KRSEPHIYVA NWFYLAFILT VAMLHIVNNL
DMPVSLFGSK SYPLFAGVQG ALVQWWYGHN AVGFFLTAGF LAMMYYFVPK QAERPIYSYR
LSIIHFWSLI FLYIWAGPHH LHYTALPDWA QTLGMVFSVM LWMPSWGGMI NGLMTLNGAW
DKVRTDPIIR MMVMALAFYG MSTFEGPMLS IKSVNSLSHY TDWTIGHVHS GALGWNGMIT
FAAVYYLAPR LWNRERLYSL RMVNWHFWLA TSGIVFYAAS MWVAGITQGL MWREYGPDGY
LVNSFADTVA ALHPMFILRA FGGLLYLSGA ILMVINVWAT ILGKLRDEVP MHDAAYDPQA
DRPILAPAE
//
