SOXA_HYDTE
ID SOXA_HYDTE Reviewed; 273 AA.
AC Q08IS0;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000269|PubMed:17516047};
DE AltName: Full=Cytochrome c551 subunit monoheme {ECO:0000250|UniProtKB:D7A6E5};
DE AltName: Full=Protein SoxA {ECO:0000303|PubMed:17516047};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000250|UniProtKB:D7A6E5, ECO:0000312|EMBL:BAF34123.1};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:17516047};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA {ECO:0000250|UniProtKB:D7A6E5};
DE Short=TOMES protein SoxA {ECO:0000250|UniProtKB:D7A6E5};
DE Flags: Precursor;
GN Name=soxA {ECO:0000312|EMBL:BAF34123.1};
OS Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila).
OC Bacteria; Proteobacteria; Hydrogenophilalia; Hydrogenophilales;
OC Hydrogenophilaceae; Hydrogenophilus.
OX NCBI_TaxID=297;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF34123.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-36, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION BY
RP THIOSULFATE, AND SIGNAL.
RC STRAIN=TH-1 / NBRC 14978 {ECO:0000312|EMBL:BAF34123.1};
RX PubMed=17516047; DOI=10.1007/s00203-007-0244-7;
RA Miyake D., Ichiki S., Tanabe M., Oda T., Kuroda H., Nishihara H.,
RA Sambongi Y.;
RT "Thiosulfate oxidation by a moderately thermophilic hydrogen-oxidizing
RT bacterium, Hydrogenophilus thermoluteolus.";
RL Arch. Microbiol. 188:199-204(2007).
CC -!- FUNCTION: C-type monoheme cytochrome, which is part of the SoxAX
CC cytochrome complex involved in sulfur oxidation. The SoxAX complex
CC catalyzes the formation of a heterodisulfide bond between the conserved
CC cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and
CC thiosulfate or other inorganic sulfur substrates. This leads to the
CC liberation of two electrons, which may be transferred from the SoxAX
CC complex to another cytochrome c that then channels them into the
CC respiratory electron transport chain. Some electrons may be used for
CC reductive CO(2) fixation. {ECO:0000250|UniProtKB:D7A6E5,
CC ECO:0000269|PubMed:17516047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] +
CC thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-
CC cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2;
CC Evidence={ECO:0000269|PubMed:17516047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY
CC protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-
CC sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689,
CC Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:140664; EC=2.8.5.2;
CC Evidence={ECO:0000269|PubMed:17516047};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:17516047};
CC Note=Binds 1 heme group per subunit. {ECO:0000269|PubMed:17516047};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000269|PubMed:17516047}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:17516047}.
CC -!- INDUCTION: By thiosulfate. {ECO:0000269|PubMed:17516047}.
CC -!- PTM: Cysteine persulfide at Cys-234. {ECO:0000250|UniProtKB:D7A6E5}.
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; AB268546; BAF34123.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08IS0; -.
DR SMR; Q08IS0; -.
DR GO; GO:0070069; C:cytochrome complex; IDA:UniProtKB.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016669; F:oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019417; P:sulfur oxidation; IDA:UniProtKB.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR025710; SoxA.
DR PIRSF; PIRSF038455; SoxA; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR TIGRFAMs; TIGR04484; thiosulf_SoxA; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Signal; Transferase; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:17516047"
FT CHAIN 25..273
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_0000423492"
FT DOMAIN 162..273
FT /note="Cytochrome c"
FT /evidence="ECO:0000255"
FT ACT_SITE 234
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT BINDING 182
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT BINDING 186
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 234
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT DISULFID 74..110
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
SQ SEQUENCE 273 AA; 30473 MW; 09BCF532D6A82F2E CRC64;
MKKTVTAVAL LCALSSTAIA PTFAADDDEA ARLKAIEEYR KQIADGNPSD LLAMEGEELW
RTPYGPKNQS LEQCDLGLGP GVVKGAAAKL PRYFPDTGKV EDLESRLMTC MERLQGVERQ
KVIDSPWRKG EKLRMDKIVA YIVTESNGEK IDVDMSHPKM KEMYELGKRM FFYRTGPFDF
SCATCHGKDG QRIRLQELPN LTKHEGAAAG WGSWPAYRVS NSQFWTMQMR LNDCFRQQRT
AEPIYGSDAT IALSVYMAAN GNGGVMLTPG IKR
