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Database: UniProt
Entry: D3ECZ4_GEOS4
LinkDB: D3ECZ4_GEOS4
Original site: D3ECZ4_GEOS4 
ID   D3ECZ4_GEOS4            Unreviewed;       632 AA.
AC   D3ECZ4;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   OrderedLocusNames=GYMC10_0737 {ECO:0000313|EMBL:ACX63037.1};
OS   Geobacillus sp. (strain Y412MC10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX63037.1, ECO:0000313|Proteomes:UP000002381};
RN   [1] {ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Brumm P., Mead D.;
RT   "Complete sequence of Geobacillus sp. Y412MC10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACX63037.1, ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX63037.1,
RC   ECO:0000313|Proteomes:UP000002381};
RX   PubMed=23408395; DOI=10.4056/sigs.2605792;
RA   Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA   Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA   Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA   Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT   "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT   Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT   Yellowstone National Park.";
RL   Stand. Genomic Sci. 6:381-400(2012).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex. CO I is the catalytic
CC       subunit of the enzyme. Electrons originating in cytochrome c are
CC       transferred via the copper A center of subunit 2 and heme A of subunit
CC       1 to the bimetallic center formed by heme A3 and copper B.
CC       {ECO:0000256|RuleBase:RU363061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029368,
CC         ECO:0000256|RuleBase:RU363061};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU363061}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363061};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363061}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU000370}.
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DR   EMBL; CP001793; ACX63037.1; -; Genomic_DNA.
DR   RefSeq; WP_009590532.1; NZ_VEAV01000007.1.
DR   AlphaFoldDB; D3ECZ4; -.
DR   STRING; 481743.GYMC10_0737; -.
DR   KEGG; gym:GYMC10_0737; -.
DR   HOGENOM; CLU_011899_7_3_9; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000002381; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01662; Ubiquinol_Oxidase_I; 1.
DR   Gene3D; 1.10.287.70; -; 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; IPR014241; Cyt_c_oxidase_su1_bac.
DR   NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF44; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
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|RuleBase:RU363061};
KW   Copper {ECO:0000256|RuleBase:RU363061};
KW   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU363061};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363061};
KW   Metal-binding {ECO:0000256|RuleBase:RU363061};
KW   Oxidoreductase {ECO:0000313|EMBL:ACX63037.1};
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|RuleBase:RU363061}; Transport {ECO:0000256|RuleBase:RU000370}.
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        71..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        108..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        158..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        196..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        242..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        312..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        349..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        383..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        466..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        559..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        590..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          14..527
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   632 AA;  70018 MW;  2E79DB28AE961724 CRC64;
     MAHAHASSHS VKRYTGIMDW LTTVDHKKIG ILYLIAGGFF FGIGGIEAIL IRLQLIKPMN
     DLVSAQVFNE LITMHGTTMI FLGVMPVIFA LMNAVIPLQI GARDVAFPFL NSLGFWTFLF
     GGLLLNLSWI MGGAPDAGWT SYTPLSTNDY SSTHGVDFYT IGLQIAGLGT LIGGINFLAT
     IITMRAPGMS FMRMPMFTWT AFITSAMILF AFPAITVGLV LLSFDRLLGA NFFDVAAGGS
     PVLWQHIFWI FGHPEVYILI LPAFGIISEV IPTFSRKRLF GYSSMVFATI LIAFLGFMVW
     AHHMFTTGLG PVANALFSIA TMLIAVPTGI KIFNWLFTMW GGQIRFTSAN LFAIGFVPTF
     VMGGVTGVML ASAPADFQFH DTYFVVAHFH YVIVGGLVFG LFAGLHYWWP KMFGRMLNET
     LGKWTFWLFA IGFHMTFFVQ HFLGLLGMQR RIVSYLPNQN FDELNFISTI GAILMGIGVL
     LFLANIAVTT RKPVGVAADP WEDGRTLEWS IPSPPPEYNF KQIPLVRGID AYWKEKMAGN
     KEMTPSEPVG PIHMPSPSIL PFVMSLGLFI AGLGFMFSTE DFSNSFMSLI FNKYIVLIVG
     LLITFAAMIA RSLYDDHGYH IEVEELEGEG KA
//
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