| Description | RecName: Full=Cytochrome c oxidase subunit 1; EC=1.9.3.1; AltName: Full=Cytochrome aa3 subunit 1; AltName: Full=Cytochrome c oxidase polypeptide I; |
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| MyHits synonyms | COX1_RHOSH
, P33517
, 65A74DBCC5C550B0
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Legends: 1, Iron (heme A axial ligand). {ECO:0000305}; 2, Copper B. {ECO:0000305}; 3, Iron (heme A3 axial ligand). {ECO:0000305}; 4, TRANSMEM Helical. {ECO:0000255}; 5, ipat:COX1_CUB [T]; 6, HELIX {ECO:0000244|PDB:3DTU}; 7, HELIX {ECO:0000244|PDB:2GSM}; 8, STRAND {ECO:0000244|PDB:2GSM}; 9, TURN {ECO:0000244|PDB:2GSM}; 10, STRAND {ECO:0000244|PDB:1M56}; 11, STRAND {ECO:0000244|PDB:3DTU}; 12, HELIX {ECO:0000244|PDB:1M56}.
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ID COX1_RHOSH Reviewed; 566 AA.
AC P33517;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 18-JAN-2017, entry version 117.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=1.9.3.1;
DE AltName: Full=Cytochrome aa3 subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=ctaD;
OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ga;
RX PubMed=1313140; DOI=10.1111/j.1365-2958.1992.tb01511.x;
RA Shapleigh J.P., Gennis R.B.;
RT "Cloning, sequencing and deletion from the chromosome of the gene
RT encoding subunit I of the aa3-type cytochrome c oxidase of Rhodobacter
RT sphaeroides.";
RL Mol. Microbiol. 6:635-642(1992).
RN [2]
RP SEQUENCE REVISION TO 436-439 AND 518-521.
RA Shapleigh J.P., Gennis R.B.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC 3 form the functional core of the enzyme complex. Co I is the
CC catalytic subunit of the enzyme. Electrons originating in
CC cytochrome c are transferred via the copper A center of subunit 2
CC and heme a of subunit 1 to the bimetallic center formed by heme a3
CC and copper B. This cytochrome c oxidase shows proton pump activity
CC across the membrane in addition to the electron transfer.
CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC ferricytochrome c + 2 H(2)O.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 copper B ion per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 2 heme groups per subunit.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
DR EMBL; X62645; CAA44514.2; -; Genomic_DNA.
DR PIR; S20534; S20534.
DR RefSeq; WP_011337048.1; NZ_CP015210.1.
DR PDB; 1M56; X-ray; 2.30 A; A/G=1-566.
DR PDB; 1M57; X-ray; 3.00 A; A/G=1-566.
DR PDB; 2GSM; X-ray; 2.00 A; A/C=1-566.
DR PDB; 3DTU; X-ray; 2.15 A; A/C=1-566.
DR PDB; 3FYE; X-ray; 2.15 A; A/C=1-566.
DR PDB; 3FYI; X-ray; 2.20 A; A/C=1-566.
DR PDBsum; 1M56; -.
DR PDBsum; 1M57; -.
DR PDBsum; 2GSM; -.
DR PDBsum; 3DTU; -.
DR PDBsum; 3FYE; -.
DR PDBsum; 3FYI; -.
DR ProteinModelPortal; P33517; -.
DR SMR; P33517; -.
DR DIP; DIP-38013N; -.
DR IntAct; P33517; 3.
DR STRING; 349102.Rsph17025_0664; -.
DR TCDB; 3.D.4.6.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR eggNOG; ENOG4105BZ9; Bacteria.
DR eggNOG; COG0843; LUCA.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P33517; -.
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:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 2.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 566 Cytochrome c oxidase subunit 1.
FT /FTId=PRO_0000183459.
FT TRANSMEM 29 49 Helical. {ECO:0000255}.
FT TRANSMEM 97 117 Helical. {ECO:0000255}.
FT TRANSMEM 141 161 Helical. {ECO:0000255}.
FT TRANSMEM 189 209 Helical. {ECO:0000255}.
FT TRANSMEM 227 247 Helical. {ECO:0000255}.
FT TRANSMEM 278 298 Helical. {ECO:0000255}.
FT TRANSMEM 310 330 Helical. {ECO:0000255}.
FT TRANSMEM 348 368 Helical. {ECO:0000255}.
FT TRANSMEM 381 401 Helical. {ECO:0000255}.
FT TRANSMEM 420 440 Helical. {ECO:0000255}.
FT TRANSMEM 455 475 Helical. {ECO:0000255}.
FT TRANSMEM 499 519 Helical. {ECO:0000255}.
FT METAL 102 102 Iron (heme A axial ligand).
FT {ECO:0000305}.
FT METAL 284 284 Copper B. {ECO:0000305}.
FT METAL 288 288 Copper B. {ECO:0000305}.
FT METAL 333 333 Copper B. {ECO:0000305}.
FT METAL 334 334 Copper B. {ECO:0000305}.
FT METAL 419 419 Iron (heme A3 axial ligand).
FT {ECO:0000305}.
FT METAL 421 421 Iron (heme A axial ligand).
FT {ECO:0000305}.
FT CROSSLNK 284 288 1'-histidyl-3'-tyrosine (His-Tyr).
FT {ECO:0000250}.
FT HELIX 16 20 {ECO:0000244|PDB:3DTU}.
FT HELIX 26 55 {ECO:0000244|PDB:2GSM}.
FT STRAND 57 59 {ECO:0000244|PDB:2GSM}.
FT STRAND 61 64 {ECO:0000244|PDB:2GSM}.
FT HELIX 65 69 {ECO:0000244|PDB:2GSM}.
FT HELIX 72 78 {ECO:0000244|PDB:2GSM}.
FT HELIX 85 87 {ECO:0000244|PDB:2GSM}.
FT HELIX 92 109 {ECO:0000244|PDB:2GSM}.
FT HELIX 111 115 {ECO:0000244|PDB:2GSM}.
FT TURN 116 118 {ECO:0000244|PDB:2GSM}.
FT HELIX 119 128 {ECO:0000244|PDB:2GSM}.
FT HELIX 136 156 {ECO:0000244|PDB:2GSM}.
FT STRAND 159 161 {ECO:0000244|PDB:1M56}.
FT HELIX 162 164 {ECO:0000244|PDB:2GSM}.
FT STRAND 165 167 {ECO:0000244|PDB:2GSM}.
FT TURN 171 174 {ECO:0000244|PDB:2GSM}.
FT HELIX 178 181 {ECO:0000244|PDB:2GSM}.
FT STRAND 183 185 {ECO:0000244|PDB:3DTU}.
FT HELIX 186 214 {ECO:0000244|PDB:2GSM}.
FT TURN 222 224 {ECO:0000244|PDB:2GSM}.
FT HELIX 227 258 {ECO:0000244|PDB:2GSM}.
FT HELIX 266 268 {ECO:0000244|PDB:2GSM}.
FT HELIX 272 306 {ECO:0000244|PDB:2GSM}.
FT HELIX 313 326 {ECO:0000244|PDB:2GSM}.
FT HELIX 331 334 {ECO:0000244|PDB:2GSM}.
FT TURN 336 339 {ECO:0000244|PDB:2GSM}.
FT HELIX 342 354 {ECO:0000244|PDB:2GSM}.
FT HELIX 356 370 {ECO:0000244|PDB:2GSM}.
FT HELIX 379 402 {ECO:0000244|PDB:2GSM}.
FT HELIX 404 410 {ECO:0000244|PDB:2GSM}.
FT HELIX 414 424 {ECO:0000244|PDB:2GSM}.
FT TURN 425 427 {ECO:0000244|PDB:2GSM}.
FT HELIX 428 444 {ECO:0000244|PDB:2GSM}.
FT STRAND 445 447 {ECO:0000244|PDB:2GSM}.
FT HELIX 450 476 {ECO:0000244|PDB:2GSM}.
FT STRAND 480 482 {ECO:0000244|PDB:2GSM}.
FT HELIX 488 490 {ECO:0000244|PDB:2GSM}.
FT HELIX 491 521 {ECO:0000244|PDB:2GSM}.
FT HELIX 538 541 {ECO:0000244|PDB:2GSM}.
FT HELIX 557 559 {ECO:0000244|PDB:1M56}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 28 503 ipfam:COX1 [T]
FT MYHIT 280 334 ipat:COX1_CUB [T]
FT MYHIT 20 558 iprf:COX1 [T]
SQ SEQUENCE 566 AA; 63147 MW; 65A74DBCC5C550B0 CRC64;
MADAAIHGHE HDRRGFFTRW FMSTNHKDIG VLYLFTGGLV GLISVAFTVY MRMELMAPGV
QFMCAEHLES GLVKGFFQSL WPSAVENCTP NGHLWNVMIT GHGILMMFFV VIPALFGGFG
NYFMPLHIGA PDMAFPRMNN LSYWLYVAGT SLAVASLFAP GGNGQLGSGI GWVLYPPLST
SESGYSTDLA IFAVHLSGAS SILGAINMIT TFLNMRAPGM TMHKVPLFAW SIFVTAWLIL
LALPVLAGAI TMLLTDRNFG TTFFQPSGGG DPVLYQHILW FFGHPEVYII VLPAFGIVSH
VIATFAKKPI FGYLPMVYAM VAIGVLGFVV WAHHMYTAGL SLTQQSYFMM ATMVIAVPTG
IKIFSWIATM WGGSIELKTP MLWALGFLFL FTVGGVTGIV LSQASVDRYY HDTYYVVAHF
HYVMSLGAVF GIFAGIYFWI GKMSGRQYPE WAGKLHFWMM FVGANLTFFP QHFLGRQGMP
RRYIDYPEAF ATWNFVSSLG AFLSFASFLF FLGVIFYTLT RGARVTANNY WNEHADTLEW
TLTSPPPEHT FEQLPKREDW ERAPAH
//
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