MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061}; EC=1.9.3.1 {ECO:0000256|RuleBase:RU363061}; |
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| MyHits synonyms | Q3J5A7_RHOS4 , Q3J5A7 , 65A74DBCC5C550B0 |
 Legends: 1, Calcium. {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}; 2, Calcium; via carbonyl oxygen. {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}; 3, Iron (heme 1 axial ligand); via tele nitrogen. {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}; 4, Copper; via pros nitrogen. {ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}; 5, Copper; via tele nitrogen. {ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}; 6, Iron (heme 2 axial ligand); via tele nitrogen. {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}; 7, TRANSMEM Helical. {ECO:0000256|RuleBase:RU363061}; 8, ipat:COX1_CUB [T].
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ID Q3J5A7_RHOS4 Unreviewed; 566 AA.
AC Q3J5A7;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 10-MAY-2017, entry version 94.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU363061};
GN Name=coxI {ECO:0000313|EMBL:ABA78027.1};
GN ORFNames=RSP_1877 {ECO:0000313|EMBL:ABA78027.1};
OS Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS 158).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272943 {ECO:0000313|EMBL:ABA78027.1, ECO:0000313|Proteomes:UP000002703};
RN [1] {ECO:0000313|Proteomes:UP000002703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
RC {ECO:0000313|Proteomes:UP000002703};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 17-551 IN COMPLEX WITH
RP CALCIUM; COPPER AND HEME, AND DISULFIDE BONDS.
RX PubMed=21205904; DOI=10.1073/pnas.1012846108;
RA Liu J., Qin L., Ferguson-Miller S.;
RT "Crystallographic and online spectral evidence for role of
RT conformational change and conserved water in cytochrome oxidase proton
RT pump.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1284-1289(2011).
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. {ECO:0000256|RuleBase:RU363061}.
CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU363061}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|RuleBase:RU363061}.
CC -!- SUBCELLULAR LOCATION: Cell membrane
CC {ECO:0000256|RuleBase:RU363061}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363061}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|RuleBase:RU363061}.
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DR EMBL; CP000143; ABA78027.1; -; Genomic_DNA.
DR RefSeq; WP_011337048.1; NZ_AKVW01000001.1.
DR RefSeq; YP_351928.1; NC_007493.2.
DR PDB; 3OM3; X-ray; 2.60 A; A/C=17-551.
DR PDB; 3OMA; X-ray; 2.30 A; A/C=17-551.
DR PDB; 3OMI; X-ray; 2.15 A; A/C=17-551.
DR PDB; 3OMN; X-ray; 2.15 A; A/C=17-551.
DR PDBsum; 3OM3; -.
DR PDBsum; 3OMA; -.
DR PDBsum; 3OMI; -.
DR PDBsum; 3OMN; -.
DR ProteinModelPortal; Q3J5A7; -.
DR SMR; Q3J5A7; -.
DR STRING; 272943.RSP_1877; -.
DR EnsemblBacteria; ABA78027; ABA78027; RSP_1877.
DR GeneID; 3719145; -.
DR KEGG; rsp:RSP_1877; -.
DR PATRIC; 23150734; VBIRhoSph57909_0767.
DR eggNOG; ENOG4105BZ9; Bacteria.
DR eggNOG; COG0843; LUCA.
DR HOGENOM; HOG000085274; -.
DR KO; K02274; -.
DR OMA; PYHTFEE; -.
DR OrthoDB; POG091H042R; -.
DR PhylomeDB; Q3J5A7; -.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; Q3J5A7; -.
DR Proteomes; UP000002703; Chromosome 1.
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; 1.
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 {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA,
KW ECO:0000213|PDB:3OMI, ECO:0000213|PDB:3OMN};
KW Calcium {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA,
KW ECO:0000213|PDB:3OMI, ECO:0000213|PDB:3OMN};
KW Cell membrane {ECO:0000256|RuleBase:RU363061};
KW Complete proteome {ECO:0000313|Proteomes:UP000002703};
KW Copper {ECO:0000213|PDB:3OMA, ECO:0000213|PDB:3OMI,
KW ECO:0000256|RuleBase:RU363061};
KW Electron transport {ECO:0000256|RuleBase:RU363061};
KW Heme {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA,
KW ECO:0000213|PDB:3OMI, ECO:0000256|RuleBase:RU363061};
KW Iron {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA,
KW ECO:0000213|PDB:3OMI, ECO:0000256|RuleBase:RU363061};
KW Membrane {ECO:0000256|RuleBase:RU363061};
KW Metal-binding {ECO:0000213|PDB:3OM3, ECO:0000213|PDB:3OMA,
KW ECO:0000213|PDB:3OMI, ECO:0000256|RuleBase:RU363061};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363061,
KW ECO:0000313|EMBL:ABA78027.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002703};
KW Respiratory chain {ECO:0000256|RuleBase:RU363061};
KW Transmembrane {ECO:0000256|RuleBase:RU363061};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363061};
KW Transport {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 29 51 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 104 123 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 143 162 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 189 215 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 227 254 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 287 306 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 313 334 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 346 369 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 381 400 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 420 440 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 452 473 Helical. {ECO:0000256|RuleBase:RU363061}.
FT TRANSMEM 493 519 Helical. {ECO:0000256|RuleBase:RU363061}.
FT DOMAIN 20 558 COX1. {ECO:0000259|PROSITE:PS50855}.
FT METAL 54 54 Calcium. {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 57 57 Calcium; via carbonyl oxygen.
FT {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 59 59 Calcium; via carbonyl oxygen.
FT {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 61 61 Calcium. {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 102 102 Iron (heme 1 axial ligand); via tele
FT nitrogen. {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 284 284 Copper; via pros nitrogen.
FT {ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 333 333 Copper; via tele nitrogen.
FT {ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 334 334 Copper; via tele nitrogen.
FT {ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 419 419 Iron (heme 2 axial ligand); via tele
FT nitrogen. {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT METAL 421 421 Iron (heme 1 axial ligand); via tele
FT nitrogen. {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
FT DISULFID 64 88 {ECO:0000213|PDB:3OM3,
FT ECO:0000213|PDB:3OMA,
FT ECO:0000213|PDB:3OMI}.
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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