SOXA_RHOSU
ID SOXA_RHOSU Reviewed; 287 AA.
AC Q939U1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000269|PubMed:11567011};
DE AltName: Full=Cytochrome c551 subunit diheme {ECO:0000303|PubMed:11567011, ECO:0000312|EMBL:AAF99434.1};
DE AltName: Full=Protein SoxA {ECO:0000303|PubMed:11567011};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000303|PubMed:11567011, ECO:0000303|PubMed:23060437};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:23060437};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA {ECO:0000303|PubMed:11523998, ECO:0000303|PubMed:12411478};
DE Short=TOMES protein SoxA {ECO:0000303|PubMed:11523998, ECO:0000303|PubMed:12411478};
DE Flags: Precursor;
GN Name=soxA {ECO:0000312|EMBL:AAF99434.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodovulum.
OX NCBI_TaxID=35806;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF99434.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-57; 66-73;
RP 132-139; 255-266 AND 274-287, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, INDUCTION BY THIOSULFATE, MASS SPECTROMETRY,
RP DISRUPTION PHENOTYPE, AND SIGNAL.
RC STRAIN=W4 {ECO:0000269|PubMed:11567011};
RX PubMed=11567011; DOI=10.1128/jb.183.20.6107-6118.2001;
RA Appia-Ayme C., Little P.J., Matsumoto Y., Leech A.P., Berks B.C.;
RT "Cytochrome complex essential for photosynthetic oxidation of both
RT thiosulfate and sulfide in Rhodovulum sulfidophilum.";
RL J. Bacteriol. 183:6107-6118(2001).
RN [2] {ECO:0000305}
RP FUNCTION, COFACTOR, EPR SPECTROSCOPY OF THE HEMES, AND MAGNETIC CIRCULAR
RP DICHROISM OF THE SOXAX COMPLEX.
RC STRAIN=W4 {ECO:0000269|PubMed:11523998};
RX PubMed=11523998; DOI=10.1021/bi0100081;
RA Cheesman M.R., Little P.J., Berks B.C.;
RT "Novel heme ligation in a c-type cytochrome involved in thiosulfate
RT oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum.";
RL Biochemistry 40:10562-10569(2001).
RN [3] {ECO:0000312|PDB:1H32}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-287 IN COMPLEXES WITH SOXX IN
RP OXIDIZED AND REDUCED STATES AND HEMES, FUNCTION, COFACTOR, SUBUNIT, EPR
RP SPECTROSCOPY OF THE HEMES, REACTION MECHANISM, ACTIVE SITE, AND CYSTEINE
RP PERSULFIDE AT CYS-248.
RC STRAIN=W4 {ECO:0000269|PubMed:12411478};
RX PubMed=12411478; DOI=10.1093/emboj/cdf566;
RA Bamford V.A., Bruno S., Rasmussen T., Appia-Ayme C., Cheesman M.R.,
RA Berks B.C., Hemmings A.M.;
RT "Structural basis for the oxidation of thiosulfate by a sulfur cycle
RT enzyme.";
RL EMBO J. 21:5599-5610(2002).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-287 IN COMPLEX WITH SOXX AND
RP HEME, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP POTENTIOMETRIC TITRATION; EPR SPECTROSCOPY AND MAGNETIC CIRCULAR DICHROISM
RP OF THE SOXAX COMPLEX, REACTION MECHANISM, ACTIVE SITE, AND CYSTEINE
RP PERSULFIDE AT CYS-248.
RC STRAIN=W4 {ECO:0000269|PubMed:23060437};
RX PubMed=23060437; DOI=10.1074/jbc.m112.396192;
RA Bradley J.M., Marritt S.J., Kihlken M.A., Haynes K., Hemmings A.M.,
RA Berks B.C., Cheesman M.R., Butt J.N.;
RT "Redox and chemical activities of the hemes in the sulfur oxidation pathway
RT enzyme SoxAX.";
RL J. Biol. Chem. 287:40350-40359(2012).
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 and which then may be used for
CC reductive CO(2) fixation. {ECO:0000269|PubMed:11523998,
CC ECO:0000269|PubMed:11567011, ECO:0000269|PubMed:12411478,
CC ECO:0000269|PubMed:23060437}.
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:11567011};
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:11567011};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:11523998, ECO:0000269|PubMed:11567011,
CC ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437};
CC Note=Binds 2 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:11523998, ECO:0000269|PubMed:11567011,
CC ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is approximately -340 mV for His/Cys(-) ligated heme (heme 1)
CC and -400 mV for His/CysS(-) ligated heme (heme 2) at pH 7.0.
CC {ECO:0000269|PubMed:23060437};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000269|PubMed:11567011,
CC ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11567011}.
CC -!- INDUCTION: By thiosulfate. {ECO:0000269|PubMed:11567011}.
CC -!- PTM: Cysteine persulfide at Cys-248. {ECO:0000269|PubMed:12411478,
CC ECO:0000269|PubMed:23060437}.
CC -!- MASS SPECTROMETRY: Mass=30177; Mass_error=4; Method=Electrospray;
CC Note=The measured mass is that of mature SoxA with a diheme bound and
CC with an undetermined modification.;
CC Evidence={ECO:0000269|PubMed:11567011};
CC -!- DISRUPTION PHENOTYPE: Unable to grow photoautotrophically on or oxidize
CC either thiosulfate or sulfide. Thiosulfate:cytochrome c oxidoreductase
CC activity is zero in periplasmic extracts prepared from cells grown on
CC thiosulfate plus malate. {ECO:0000269|PubMed:11567011}.
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255, ECO:0000305}.
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DR EMBL; AY005800; AAF99434.1; -; Genomic_DNA.
DR RefSeq; WP_042460802.1; NZ_CP015421.1.
DR PDB; 1H31; X-ray; 2.55 A; A/C/E/G=27-287.
DR PDB; 1H32; X-ray; 1.50 A; A=27-287.
DR PDB; 1H33; X-ray; 1.75 A; A=27-287.
DR PDB; 2OZ1; X-ray; 2.35 A; A/C/E/G=27-287.
DR PDBsum; 1H31; -.
DR PDBsum; 1H32; -.
DR PDBsum; 1H33; -.
DR PDBsum; 2OZ1; -.
DR AlphaFoldDB; Q939U1; -.
DR SMR; Q939U1; -.
DR STRING; 1188256.BASI01000002_gene3425; -.
DR GeneID; 62371232; -.
DR eggNOG; COG3258; Bacteria.
DR BRENDA; 2.8.5.2; 5384.
DR EvolutionaryTrace; Q939U1; -.
DR GO; GO:0070069; C:cytochrome complex; IGC:UniProtKB.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0016783; F:sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0019418; P:sulfide oxidation; IMP:UniProtKB.
DR GO; GO:0019417; P:sulfur oxidation; IMP: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 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Signal; Transferase; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11567011"
FT CHAIN 27..287
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /id="PRO_0000423489"
FT DOMAIN 74..168
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 248
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:12411478,
FT ECO:0000269|PubMed:23060437"
FT BINDING 102
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 105
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 106
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:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 140
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:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 203
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 206
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 207
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:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12411478"
FT BINDING 248
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:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2OZ1"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1H32"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:1H32"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1H32"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2OZ1"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:1H32"
SQ SEQUENCE 287 AA; 31332 MW; 95748C569D40853F CRC64;
MKTMTGRLVA AALVCGGAFS GAAVSAGPDD PLVINGEIEI VTRAPTPAHL ADRFDEIRSG
WTFRTDDTQA LEMDDFENSG MVFVEEARAV WDRPEGTEGK ACADCHGAVD DGMYGLRAVY
PKYVESAGKV RTVEQMINAC RTSRMGAPEW DYIGPDMTAM VALIASVSRG MPVSVAIDGP
AQSTWEKGRE IYYTRYGQLD LSCASCHEQY FDHYIRADHL SQGQINGFPS YRLKNARLNA
VHDRFRGCIR DTRGVPFAVG SPEFVALELY VASRGNGLSV EGPSVRN
