CYOA_HAEIN
ID CYOA_HAEIN Reviewed; 521 AA.
AC P45021;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable cytochrome oxidase subunit 1;
DE Short=Cytochrome oxidase subunit I;
DE EC=1.10.3.-;
GN OrderedLocusNames=HI_1076;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Probable cytochrome oxidase subunit.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=May bind up to 3 heme groups per complex. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of subunits I and II. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Probable ortholog of the ancestor of E.coli AppC/CydA.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC22732.1; -; Genomic_DNA.
DR PIR; E64181; E64181.
DR RefSeq; NP_439232.1; NC_000907.1.
DR RefSeq; WP_010869127.1; NC_000907.1.
DR AlphaFoldDB; P45021; -.
DR SMR; P45021; -.
DR STRING; 71421.HI_1076; -.
DR EnsemblBacteria; AAC22732; AAC22732; HI_1076.
DR KEGG; hin:HI_1076; -.
DR PATRIC; fig|71421.8.peg.1118; -.
DR eggNOG; COG1271; Bacteria.
DR HOGENOM; CLU_030555_3_1_6; -.
DR OMA; FLINIAM; -.
DR PhylomeDB; P45021; -.
DR BioCyc; HINF71421:G1GJ1-1110-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..521
FT /note="Probable cytochrome oxidase subunit 1"
FT /id="PRO_0000183923"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..94
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..187
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..397
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..521
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 521 AA; 58137 MW; FD444C20457D2265 CRC64;
MLDVVDLSRL QFALTALYHF IFVPLTLGLS FILVIMETIY VATGKEVYKD MTKFWGKLFG
INFALGVTTG IIMEFQFGTN WSYYSHYVGD IFGAPLAIEA LLAFFLESTF VGLFFFGWDR
LSKGKHLLAT YCVAFGSNLS AMWILVANGW MQAPTGSEFN FETVRMEMTN FLDLWLNPVA
QSKFLHTLSA GYVTGAFFVL AISSYFLLKG RDFEFAKRSF SVAATFGFIA SISVLILGDE
SGYDIGKAQP VKLAAMEAEF ETHPAPAPFL PVAIPNTAEM KNDFAIEIPY LGGVIATRSI
DKEIIGLKDL QALNETRVRS GIRAYELFTQ LRAEKKANGQ VNEETKAQFN EVKKDLGFGL
LLKRYTNNVV DATEEQIKQA ARDTIPNVGP NFWAFRAMIA AGGLIALLTF GAFVQNLRNK
VTQIPLLLKV LLWGLPLPWI AIECGWFLAE YGRQPWATYE ILPVGVSASN LSTGDLWFSI
GLICALYLAF IIVEMYLMFK YARLGPSALK TGKYYFEQSA K
