QOX1_SULAC
ID QOX1_SULAC Reviewed; 517 AA.
AC P98004; Q4J749;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Quinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Cytochrome aa3 subunit 1;
DE AltName: Full=Oxidase aa(3) subunit 1;
DE AltName: Full=Quinol oxidase polypeptide I;
GN Name=soxB; OrderedLocusNames=Saci_2088;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=1372250; DOI=10.1002/j.1460-2075.1992.tb05117.x;
RA Luebben M., Kolmerer B., Saraste M.;
RT "An archaebacterial terminal oxidase combines core structures of two
RT mitochondrial respiratory complexes.";
RL EMBO J. 11:805-812(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
CC -!- FUNCTION: Catalyzes the reduction of oxygen to water.
CC -!- FUNCTION: Subunits I, II and III form the functional core of the enzyme
CC complex. Electrons originating in caldariella quinol are transferred to
CC the binuclear center formed by heme A3 and Cu(B).
CC -!- FUNCTION: Subunit I binds heme a and the bimetallic center.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:132124;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY81382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X62643; CAA44510.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY81382.1; ALT_INIT; Genomic_DNA.
DR PIR; S21042; S21042.
DR RefSeq; WP_015385766.1; NC_007181.1.
DR AlphaFoldDB; P98004; -.
DR SMR; P98004; -.
DR STRING; 330779.Saci_2088; -.
DR TCDB; 3.D.4.1.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR EnsemblBacteria; AAY81382; AAY81382; Saci_2088.
DR GeneID; 3472601; -.
DR KEGG; sai:Saci_2088; -.
DR PATRIC; fig|330779.12.peg.2090; -.
DR eggNOG; arCOG01238; Archaea.
DR HOGENOM; CLU_534881_0_0_2; -.
DR BioCyc; MetaCyc:MON-21018; -.
DR BRENDA; 7.1.1.4; 6160.
DR Proteomes; UP000001018; Chromosome.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; ISS:UniProtKB.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; ISS:UniProtKB.
DR Gene3D; 1.20.210.10; -; 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 PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..517
FT /note="Quinol oxidase subunit 1"
FT /id="PRO_0000183475"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 235
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 239
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 285
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 372
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 374
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 235..239
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT CONFLICT 478
FT /note="A -> R (in Ref. 1; CAA44510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 57808 MW; 5EF4EF051BD89CC7 CRC64;
MSLIERIKNV VWPKDTLSVV WLYTIGSIFW LGVLGIAAMN LRTFLTYDQN SPNVGELYYS
ALTIHGWAAM IAFVPMAAAA VIGFSLYKSK LSIIHTKQMA IFFWLSNVLL GIAMAGSPDM
GWYMYPPLAI ESNSQFHAFL FYTTPQLMGM AYLVMSIAVI LQTAAFVTLI ADAYATKPKG
ERLNIFAAYG VAFSIVIAVT LPALAAATLW YTLYFFANVP VNNLLWAILF WFYGHPVVYY
VPFPLFGALY YYIPQYAGRS LYSEKWARWN IYLLAIGTMG VWVHHLQTWP LPIVLREWVN
LSTLILATGS GLTVLNLGLT IFTSRKYDWK DPVGMGALIS LIGFILAGAQ ALVLPENSIN
PLFHNSYYVV GHFHLMIWTL IIMGYTTVFL DMLRTSFAGF NFSATSSKWM RIGMIWWTAP
FMGVGYAMSV AGYLGFLRRM IAYPVIFQPY NLVESFLAEI GIPGLLLTLF VGMFDALAYA
SKQPVFSSPS VSSFSMQVDK GELVKKIDSE KGVNNVG
