SOXA2_HYDTT
ID SOXA2_HYDTT Reviewed; 259 AA.
AC D3DJG5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
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:BAI69967.1};
DE AltName: Full=Protein SoxA2 {ECO:0000303|PubMed:20378963};
DE AltName: Full=SoxAX cytochrome complex subunit A2;
DE AltName: Full=Sulfur oxidizing protein A2 {ECO:0000303|PubMed:20378963, ECO:0000312|EMBL:ADO45890.1};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA2;
DE Short=TOMES protein SoxA2;
DE Flags: Precursor;
GN Name=soxA2 {ECO:0000312|EMBL:BAI69967.1};
GN OrderedLocusNames=HTH_1518, Hydth_1506;
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:BAI69967.1}
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-220. {ECO:0000250|UniProtKB:O33434}.
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; AP011112; BAI69967.1; -; Genomic_DNA.
DR EMBL; CP002221; ADO45890.1; -; Genomic_DNA.
DR RefSeq; WP_012964147.1; NC_017161.1.
DR AlphaFoldDB; D3DJG5; -.
DR SMR; D3DJG5; -.
DR STRING; 608538.HTH_1518; -.
DR EnsemblBacteria; BAI69967; BAI69967; HTH_1518.
DR KEGG; hte:Hydth_1506; -.
DR KEGG; hth:HTH_1518; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_079910_1_0_0; -.
DR OMA; PIYRSEW; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..259
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_5000650632"
FT DOMAIN 50..135
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 220
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 70
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 73
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 74
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 108
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 171
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 174
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 175
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 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 220
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 259 AA; 29659 MW; EF553CAFD2A83846 CRC64;
MRKLWFLPIL LGAVGGVSLY AIAQQENPAE EVKKQKELLL KEMGILPGDV YAEQGRDMFN
KPMGNAGKSC SSCHGQDGRY LRGAYAHMPR YYKDMDAVAD LDTRIKYCME KYMGVGNVKH
DLNFKSIATY VATLSNGMKM DVKLTHPKER EMYEKGRELW YARVGKMDFS CAICHDTFGG
QRIRLQTLAK VKEDKVATHW PAYRFSNDQL WTMEDRIRGC YNQIRVTPPP HFSWPQIALS
LYMAYESKGG TIETPGFVR
