QOXM_SULAC
ID QOXM_SULAC Reviewed; 788 AA.
AC P39481; Q4J6N2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Quinol oxidase subunit 1/3;
DE EC=1.10.3.-;
DE AltName: Full=Quinol oxidase polypeptide I/III;
GN Name=soxM; OrderedLocusNames=Saci_2263;
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=8076636; DOI=10.1111/j.1432-1033.1994.tb20006.x;
RA Luebben M., Arnaud S., Castresana J., Warne A., Albracht S.P.J.,
RA Saraste M.;
RT "A second terminal oxidase in Sulfolobus acidocaldarius.";
RL Eur. J. Biochem. 224:151-159(1994).
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: Terminal oxidase is the component of the respiratory chain
CC that catalyzes the reduction of oxygen to water. SoxM forms the
CC functional core of the enzyme complex.
CC -!- FUNCTION: Catalytic subunit of the enzyme. Electrons originating in a
CC quinol are transferred to the bimetallic center of SoxM formed by a
CC heme and copper B.
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 -!- 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 -!- SUBUNIT: Forms a complex with at least SoxC and a 30 kDa Rieske Fe-S
CC protein, but neither with SoxA nor SoxB.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: SoxM is probably a precursor form of subunits I and III.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 3 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; X73567; CAA51969.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY81549.1; -; Genomic_DNA.
DR PIR; S48191; S48191.
DR RefSeq; WP_011279051.1; NC_007181.1.
DR AlphaFoldDB; P39481; -.
DR SMR; P39481; -.
DR STRING; 330779.Saci_2263; -.
DR EnsemblBacteria; AAY81549; AAY81549; Saci_2263.
DR GeneID; 3474524; -.
DR KEGG; sai:Saci_2263; -.
DR PATRIC; fig|330779.12.peg.2272; -.
DR eggNOG; arCOG01237; Archaea.
DR HOGENOM; CLU_011899_7_1_2; -.
DR OMA; LMMATTI; -.
DR BioCyc; MetaCyc:MON-21016; -.
DR BRENDA; 7.1.1.4; 6160.
DR UniPathway; UPA00705; -.
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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.120.80; -; 1.
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 InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR Pfam; PF00510; COX3; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
DR PROSITE; PS50253; COX3; 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..788
FT /note="Quinol oxidase subunit 1/3"
FT /id="PRO_0000183905"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 62
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 238
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 242
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 288
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 289
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 374
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 376
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 238..242
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 788 AA; 87082 MW; 3939C16CDB8A08AD CRC64;
MNIKRILKVA LYTTNASDVG QMYIVLGIVA LIIGSVNAAL IRDQLSFNNL NAVDYYDAVT
LHGIFMIFFV VMPLSTGFAN YLVPRMIGAH DLYWPKINAL SFWMLVPAVI LAAISPLLGA
VDLGWYMYAP LSVETTVNYG LGTNLIQIAL ILSGLSSTLT GVNFVMTITK MKKVPYLKMP
LFVWGFFTTA ILMIIAMPSL TAGLVFAYLE RLWGTPFFDS ALGGSPVLWQ QLFWFFGHPE
VYILILPAMG LVSELLPKMA RREIFGYTAI ALSSIAIAFL SALGVWMHHM FTAIDNTLVQ
IVSSATTMAI AIPSGVKVLN WTATLYGGEI RYKTPTILLI SFIVMFLLGG ITGVFFPLVP
IDYALNGTYF VVGHFHYMVY AILYALLGAL FYYFPFWSGK WYNDDLGKTG AILLVAGTFL
TATGMSIAGI LGMPRRYAVI PSPIYDPFQF MASVGAVLTG IGLFILAGVL VHGVFRGRAV
NGVDPWDNIS VKLQDFFIKP VKLPLSFGKS LDGAFDEEYH GIKFPYYSVL GLFLSFIPLG
FMFILIGLIP IGIVLLLAFM GVGLYWGYDQ WFKPMQPPPH FYADGGVPVT NSVNNSISPS
LGIASMRDAR SAVLWFILAE VILFGSFIGG YAFIMSPVTN PLSYVNNIVP AVEVFPLPAI
MTAILLSSSI PAHIAYEYFK KGNVKMFRNL GLLTMAMGLT FLGGQIYEFT HYIHFIPQDS
AASSFFFATV SLHGFHVIMG LVIWAFMMLR IRKGFIPYAG SVAATYYWHF VDAVWVVVFS
TFYLHLIV
