SOXA1_HYDTT
ID SOXA1_HYDTT Reviewed; 253 AA.
AC D3DJG4;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000269|PubMed:20378963};
DE AltName: Full=Cytochrome c551 subunit diheme {ECO:0000250|UniProtKB:O33434, ECO:0000312|EMBL:BAI69966.1};
DE AltName: Full=Protein SoxA1 {ECO:0000303|PubMed:20378963};
DE AltName: Full=SoxAX cytochrome complex subunit A1;
DE AltName: Full=Sulfur oxidizing protein A1 {ECO:0000303|PubMed:20378963, ECO:0000312|EMBL:ADO45889.1};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA1;
DE Short=TOMES protein SoxA1;
DE Flags: Precursor;
GN Name=soxA1 {ECO:0000312|EMBL:BAI69966.1};
GN OrderedLocusNames=HTH_1517, Hydth_1505;
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter.
OX NCBI_TaxID=608538;
RN [1] {ECO:0000312|EMBL:BAI69966.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=20348262; DOI=10.1128/jb.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=21677850; DOI=10.4056/sigs.1463589;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., Tice H.,
RA Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Ngatchou-Djao O.D., Land M., Hauser L., Jeffries C.D.,
RA Han C., Detter J.C., Ubler S., Rohde M., Tindall B.J., Goker M., Wirth R.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Hydrogenobacter thermophilus type strain (TK-
RT 6).";
RL Stand. Genomic Sci. 4:131-143(2011).
RN [3] {ECO:0000305}
RP PROBABLE FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 6534 / IAM 12695 / TK-6 {ECO:0000269|PubMed:20378963};
RX PubMed=20378963; DOI=10.1271/bbb.90948;
RA Sano R., Kameya M., Wakai S., Arai H., Igarashi Y., Ishii M., Sambongi Y.;
RT "Thiosulfate oxidation by a thermo-neutrophilic hydrogen-oxidizing
RT bacterium, Hydrogenobacter thermophilus.";
RL Biosci. Biotechnol. Biochem. 74:892-894(2010).
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:O33434,
CC ECO:0000269|PubMed:20378963}.
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:20378963};
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:20378963};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:O33434};
CC Note=Binds 2 heme c groups covalently per subunit.
CC {ECO:0000250|UniProtKB:O33434};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000250|UniProtKB:O33434}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:O33434}.
CC -!- PTM: Cysteine persulfide at Cys-214. {ECO:0000250|UniProtKB:O33434}.
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; AP011112; BAI69966.1; -; Genomic_DNA.
DR EMBL; CP002221; ADO45889.1; -; Genomic_DNA.
DR RefSeq; WP_012964146.1; NC_017161.1.
DR AlphaFoldDB; D3DJG4; -.
DR SMR; D3DJG4; -.
DR STRING; 608538.HTH_1517; -.
DR EnsemblBacteria; BAI69966; BAI69966; HTH_1517.
DR KEGG; hte:Hydth_1505; -.
DR KEGG; hth:HTH_1517; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_079910_0_0_0; -.
DR OMA; RTMQHRL; -.
DR OrthoDB; 1297285at2; -.
DR Proteomes; UP000002574; Chromosome.
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; IGC: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; IGC:UniProtKB.
DR GO; GO:0016669; F:oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor; IGC:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019417; P:sulfur oxidation; IGC:UniProtKB.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
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.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transferase; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..253
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_5000650631"
FT DOMAIN 44..129
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 214
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 68
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 102
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 165
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 168
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q939U1,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 169
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 214
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 253 AA; 29025 MW; 999DB7A315BBA046 CRC64;
MGKWVTIIFV LFLYAIAQQE NPAEEVKKQK ELLLKEMGIL PGDVYAEQGR DMFNKPMGNA
GKSCSSCHGQ DGRYLRGAYA HMPRYYKDMD AVADLDTRIK YCMEKYMGVG NVKHDLNFKS
IATYVATLSN GMKMDVKLTH PKEREMYEKG RELWYARVGK MDFSCAICHD SEAGKRVFLQ
TVVAVKEDKV ATHWPAYRFS NDQLWTMEDR IRGCFGDMRV APPEHFHWAV VALNLYLSYK
AKGGVVRVPG FIY
