SOXA_CHLTI
ID SOXA_CHLTI Reviewed; 286 AA.
AC Q8RLX0;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000250|UniProtKB:D7A6E5};
DE AltName: Full=Cytochrome c551 subunit monoheme {ECO:0000303|PubMed:11863431, ECO:0000303|PubMed:9692944};
DE AltName: Full=Protein SoxA {ECO:0000303|PubMed:11863431};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000312|EMBL:AAL68886.1};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:11863431};
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:AAL68886.1};
OS Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp.
OS thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=115852;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL68886.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, SUBCELLULAR
RP LOCATION, AND INDUCTION BY THIOSULFATE.
RC STRAIN=DSM 249 / 6230 / Tassajara {ECO:0000269|PubMed:11863431};
RX PubMed=11863431; DOI=10.1021/bi011404m;
RA Verte F., Kostanjevecki V., De Smet L., Meyer T.E., Cusanovich M.A.,
RA Van Beeumen J.J.;
RT "Identification of a thiosulfate utilization gene cluster from the green
RT phototrophic bacterium Chlorobium limicola.";
RL Biochemistry 41:2932-2945(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 29-286, FUNCTION, COFACTOR, CYSTEINE PERSULFIDE AT
RP CYS-247, MASS SPECTROMETRY, SIGNAL, AND DISULFIDE BOND.
RC STRAIN=NCIB 8346 {ECO:0000305};
RX PubMed=9692944; DOI=10.1021/bi9806706;
RA Klarskov K., Verte F., Van Driessche G., Meyer T.E., Cusanovich M.A.,
RA Van Beeumen J.;
RT "The primary structure of soluble cytochrome c-551 from the phototrophic
RT green sulfur bacterium Chlorobium limicola, strain Tassajara, reveals a
RT novel c-type cytochrome.";
RL Biochemistry 37:10555-10562(1998).
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 and which then may be used for
CC reductive CO(2) fixation. {ECO:0000250|UniProtKB:Q939U1,
CC ECO:0000269|PubMed:11863431, ECO:0000269|PubMed:9692944}.
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:D7A6E5};
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:D7A6E5};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:D7A6E5, ECO:0000269|PubMed:11863431,
CC ECO:0000269|PubMed:9692944};
CC Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:D7A6E5,
CC ECO:0000269|PubMed:11863431, ECO:0000269|PubMed:9692944};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. The SoxAX complex interacts with
CC CT1020, SoxAX-binding protein SaxB (SoxK); this interaction stimulates
CC catalytic activity of the complex (By similarity).
CC {ECO:0000250|UniProtKB:D7A6E5, ECO:0000250|UniProtKB:Q8KDM7}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11863431}.
CC -!- INDUCTION: By thiosulfate. {ECO:0000269|PubMed:11863431}.
CC -!- PTM: Cysteine persulfide at Cys-247. {ECO:0000250|UniProtKB:D7A6E5,
CC ECO:0000269|PubMed:9692944}.
CC -!- MASS SPECTROMETRY: Mass=29903.8; Method=Electrospray; Note=The measured
CC mass is that of mature SoxA with a heme bound, a cysteic acid residue
CC at position 247 and a disulfide bridge.;
CC Evidence={ECO:0000269|PubMed:9692944};
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; AY074395; AAL68886.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RLX0; -.
DR SMR; Q8RLX0; -.
DR GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
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:0004792; F:thiosulfate sulfurtransferase activity; IDA:UniProtKB.
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..28
FT /evidence="ECO:0000269|PubMed:9692944"
FT CHAIN 29..286
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_0000423490"
FT DOMAIN 180..286
FT /note="Cytochrome c"
FT /evidence="ECO:0000255, ECO:0000305"
FT ACT_SITE 247
FT /note="Cysteine persulfide intermediate"
FT BINDING 200
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D7A6E5"
FT BINDING 204
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 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 247
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 106..137
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 29..30
FT /note="VN -> TD (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 33
FT /note="A -> K (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 39..41
FT /note="VKK -> TQA (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 44
FT /note="G -> S (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 47
FT /note="L -> Q (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 52
FT /note="G -> E (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 56
FT /note="E -> A (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 59..60
FT /note="GD -> AN (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 69
FT /note="S -> A (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 71
FT /note="K -> T (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 74
FT /note="K -> Q (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 104
FT /note="G -> A (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 108..109
FT /note="SN -> PD (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 116
FT /note="M -> Q (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 125
FT /note="K -> G (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 128
FT /note="I -> V (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 140
FT /note="A -> K (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 145..149
FT /note="PYAPK -> AWPWQ (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 153
FT /note="I -> L (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 155
FT /note="R -> K (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 160
FT /note="I -> M (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 162
FT /note="S -> Y (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 169
FT /note="I -> V (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 187..188
FT /note="EM -> KF (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 208
FT /note="S -> A (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 217
FT /note="I -> V (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 223
FT /note="H -> Q (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 249
FT /note="E -> K (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 261
FT /note="K -> E (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 272
FT /note="V -> A (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
FT VARIANT 278..279
FT /note="KF -> EY (in strain: NCIB 8346)"
FT /evidence="ECO:0000269|PubMed:9692944"
SQ SEQUENCE 286 AA; 32026 MW; 874334F3CD85EABE CRC64;
MKKTIQRGLF TGALVLLTAM TSKPAHAAVN YQALVDADVK KFQGYFLKEF PGVKLEDFGD
GVYALDEDSR KQWKEMEEFP PYELDVEAGK ALFNKPFANG KSLGSCFSNG GAVRGMYPYF
DEKRKEVITL EMAINECRVA NGEKPYAPKK GDIARVSAYI ASISRGQKID VKVKSKAAYD
AYMKGKEMFY AKRGQLNMSC SGCHMEYSGR HLRAEIISPA LGHTTHFPVF RSKWGEIGTL
HRRYAGCNEN IGAKPFPAQS KEYRDLEFFQ TVMSNGLKFN GPASRK
