SOXA_PSESE
ID SOXA_PSESE Reviewed; 286 AA.
AC Q9K4M4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000269|PubMed:10894738};
DE AltName: Full=Cytochrome c551 subunit diheme {ECO:0000250|UniProtKB:Q939U1};
DE AltName: Full=Protein SoxA {ECO:0000303|PubMed:10894738};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000250|UniProtKB:Q939U1, ECO:0000312|EMBL:CAB94219.2};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:10894738};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA {ECO:0000250|UniProtKB:Q939U1};
DE Short=TOMES protein SoxA {ECO:0000250|UniProtKB:Q939U1};
DE Flags: Precursor;
GN Name=soxA {ECO:0000312|EMBL:CAB94219.2};
OS Pseudaminobacter salicylatoxidans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Pseudaminobacter.
OX NCBI_TaxID=93369;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB94219.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION
RP BY THIOSULFATE, AND DISRUPTION PHENOTYPE.
RC STRAIN=KCT001 {ECO:0000312|EMBL:CAB94219.2};
RX PubMed=10894738; DOI=10.1128/jb.182.15.4278-4287.2000;
RA Mukhopadhyaya P.N., Deb C., Lahiri C., Roy P.;
RT "A soxA gene, encoding a diheme cytochrome c, and a sox locus, essential
RT for sulfur oxidation in a new sulfur lithotrophic bacterium.";
RL J. Bacteriol. 182:4278-4287(2000).
CC -!- FUNCTION: C-type diheme 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:10894738}.
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:10894738};
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:10894738};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q939U1};
CC Note=Binds 2 heme groups per subunit. {ECO:0000250|UniProtKB:Q939U1};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000250|UniProtKB:Q939U1}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q939U1}.
CC -!- INDUCTION: By thiosulfate. {ECO:0000269|PubMed:10894738}.
CC -!- PTM: Cysteine persulfide at Cys-247. {ECO:0000250|UniProtKB:Q939U1}.
CC -!- DISRUPTION PHENOTYPE: Impaired in oxidation of sulfur compounds.
CC {ECO:0000269|PubMed:10894738}.
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; AJ404005; CAB94219.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9K4M4; -.
DR SMR; Q9K4M4; -.
DR STRING; 1192868.CAIU01000015_gene1958; -.
DR GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IMP:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IMP:UniProtKB.
DR GO; GO:0016669; F:oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor; IMP:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019417; P:sulfur oxidation; IMP: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 Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW Transferase; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..286
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_5000067909"
FT DOMAIN 80..166
FT /note="Cytochrome c"
FT /evidence="ECO:0000255"
FT ACT_SITE 247
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 100
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 104
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 138
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 202
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 205
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 206
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 247
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
SQ SEQUENCE 286 AA; 31579 MW; 3367E2DD928EDD9C CRC64;
MTVSKRFLAP VFAMVGGLVL AFSANADPVD EELVIDDIPM VTRAAAPEGH PFDEGLSGWL
FREAETRETE ADSFANPGML AVERGADIWN TVEGSAGKSC ASCHDDAATS MKNVGAQYPK
WDADAKRPIN IELQIDKCRV ENMGAEPYKF DAEGQVALTS YIKHQSLGTP VKMDLSDGEL
QDWWEKGKEL YYTRTGQLNF ACASCHEDSM GKYIRADHLS QGQANGFPTY RFNTGGMVSL
HNRFRGCIRD TRAEMPKAFS DELMALEVYV TWRGTGLSVE TPAVRQ
