SOXA_ALLVI
ID SOXA_ALLVI Reviewed; 281 AA.
AC Q1W3E4;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA;
DE EC=2.8.5.2 {ECO:0000250|UniProtKB:Q8KDM7};
DE AltName: Full=Cytochrome c550 subunit monoheme {ECO:0000303|PubMed:16995898};
DE AltName: Full=Protein SoxA {ECO:0000312|EMBL:ABE01361.1};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000250|UniProtKB:Q8RLX0};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:16995898};
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:ABE01361.1};
OS Allochromatium vinosum (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=1049;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABE01361.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, SUBUNIT, INDUCTION
RP BY THIOSULFATE, AND DISRUPTION PHENOTYPE.
RX PubMed=16995898; DOI=10.1111/j.1365-2958.2006.05408.x;
RA Hensen D., Sperling D., Trueper H.G., Brune D.C., Dahl C.;
RT "Thiosulphate oxidation in the phototrophic sulphur bacterium
RT Allochromatium vinosum.";
RL Mol. Microbiol. 62:794-810(2006).
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 intermediary formation of conspicuous sulfur globules inside of the
CC cells. {ECO:0000250|UniProtKB:Q8KDM7, ECO:0000269|PubMed:16995898}.
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:0000250|UniProtKB:Q8KDM7};
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:0000250|UniProtKB:Q8KDM7};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q8KDM7, ECO:0000269|PubMed:16995898};
CC Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:Q8KDM7,
CC ECO:0000269|PubMed:16995898};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000269|PubMed:16995898}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q8KDM7}.
CC -!- INDUCTION: By thiosulfate. {ECO:0000269|PubMed:16995898}.
CC -!- PTM: Cysteine persulfide at Cys-242. {ECO:0000250|UniProtKB:Q8RLX0}.
CC -!- DISRUPTION PHENOTYPE: No oxidation of thiosulfate with a simultaneous
CC deletion of soxX alone or together with a deletion of soxB.
CC {ECO:0000269|PubMed:16995898}.
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; DQ441405; ABE01361.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1W3E4; -.
DR SMR; Q1W3E4; -.
DR OMA; PIYRSEW; -.
DR BioCyc; MetaCyc:MON-16066; -.
DR BRENDA; 2.8.5.2; 257.
DR GO; GO:0070069; C:cytochrome complex; IDA:UniProtKB.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IGI: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; IGI:UniProtKB.
DR GO; GO:0016669; F:oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor; IGI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019417; P:sulfur oxidation; IGI: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 Disulfide bond; Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Signal; Transferase; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..281
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_5000006509"
FT DOMAIN 175..281
FT /note="Cytochrome c"
FT /evidence="ECO:0000255"
FT ACT_SITE 242
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT BINDING 195
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT BINDING 199
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 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 242
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 99..130
FT /evidence="ECO:0000250|UniProtKB:Q8RLX0"
SQ SEQUENCE 281 AA; 31730 MW; 01F691A98E618881 CRC64;
MTKHGFLLAT LVLAGATLPI GPVTAATPEE EQAAFQAYFK QRFPNVPEDE FKNGTYAIDP
VTRENWEAIE EFPPYENAIS QGETLWNTPF ADGQGYADCF PDGPAIMNHY PRWDRERGQV
MTLPLALNAC RTAHGETPLK YKKGPIADLL AYIAFESRGQ ITRVEIPQDD PRALAAYEQG
KRFYFARRGQ LNFACAHCHL ATSGTKLRTE TLSPAYGHTT HWPVYRSEWG EMGTLHRRFA
GCNEQVRAKA FEPQGEEYRN LEYFLTYMNN GLELNGPGAR K
