SOXA_PARPN
ID SOXA_PARPN Reviewed; 290 AA.
AC O33434;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000305};
DE EC=2.8.5.2 {ECO:0000269|PubMed:10940005};
DE AltName: Full=Cytochrome c551 subunit diheme {ECO:0000250|UniProtKB:Q939U1};
DE AltName: Full=Protein SoxA {ECO:0000312|EMBL:CAA55827.2};
DE AltName: Full=SoxAX cytochrome complex subunit A {ECO:0000303|PubMed:10940005, ECO:0000303|PubMed:16297640, ECO:0000303|PubMed:17547421};
DE AltName: Full=Sulfur oxidizing protein A {ECO:0000303|PubMed:16297640, ECO:0000303|PubMed:17547421};
DE AltName: Full=Thiosulfate-oxidizing multienzyme system protein SoxA {ECO:0000250|UniProtKB:Q939U1, ECO:0000303|PubMed:10940005};
DE Short=TOMES protein SoxA {ECO:0000250|UniProtKB:Q939U1};
DE Flags: Precursor;
GN Name=soxA {ECO:0000312|EMBL:CAA55827.2};
OS Paracoccus pantotrophus (Thiosphaera pantotropha).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=82367;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-50; 59-69;
RP 181-188 AND 212-220, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND SIGNAL.
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC 82005 / GB17;
RX PubMed=10940005; DOI=10.1128/jb.182.17.4677-4687.2000;
RA Friedrich C.G., Quentmeier A., Bardischewsky F., Rother D., Kraft R.,
RA Kostka S., Prinz H.;
RT "Novel genes coding for lithotrophic sulfur oxidation of Paracoccus
RT pantotrophus GB17.";
RL J. Bacteriol. 182:4677-4687(2000).
RN [2] {ECO:0000305}
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP POTENTIOMETRIC TITRATION AND EPR SPECTROSCOPY OF THE SOXAX COMPLEX.
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC 82005 / GB17;
RX PubMed=17547421; DOI=10.1021/bi7003526;
RA Reijerse E.J., Sommerhalter M., Hellwig P., Quentmeier A., Rother D.,
RA Laurich C., Bothe E., Lubitz W., Friedrich C.G.;
RT "The unusal redox centers of SoxXA, a novel c-type heme-enzyme essential
RT for chemotrophic sulfur-oxidation of Paracoccus pantotrophus.";
RL Biochemistry 46:7804-7810(2007).
RN [3] {ECO:0000305, ECO:0000312|PDB:2C1D}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 27-290 IN COMPLEX WITH HEME; ZINC
RP AND SOXX, FUNCTION, COFACTOR, SUBUNIT, ACTIVE SITE, AND CYSTEINE PERSULFIDE
RP AT CYS-251.
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC 82005 / GB17;
RX PubMed=16297640; DOI=10.1016/j.jsb.2005.09.002;
RA Dambe T., Quentmeier A., Rother D., Friedrich C., Scheidig A.J.;
RT "Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a
RT heme enzyme initiating chemotrophic sulfur oxidation.";
RL J. Struct. Biol. 152:229-234(2005).
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:0000269|PubMed:10940005,
CC ECO:0000269|PubMed:16297640, ECO:0000269|PubMed:17547421}.
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:10940005};
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:10940005};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:16297640,
CC ECO:0000269|PubMed:17547421};
CC Note=Binds 2 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:16297640,
CC ECO:0000269|PubMed:17547421};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16297640};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16297640};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.034 uM for thiosulfate using purified SoxAX complex (at pH 7.5)
CC {ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:17547421};
CC Redox potential:
CC E(0) is -432 for heme 2 at pH 7.0. This transition depends on pH by
CC approximately -45 mV/pH unit. {ECO:0000269|PubMed:10940005,
CC ECO:0000269|PubMed:17547421};
CC -!- SUBUNIT: Heterodimer of SoxA and SoxX. {ECO:0000269|PubMed:10940005,
CC ECO:0000269|PubMed:16297640, ECO:0000269|PubMed:17547421}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10940005,
CC ECO:0000305|PubMed:17547421}.
CC -!- PTM: Cysteine persulfide at Cys-251. {ECO:0000269|PubMed:16297640}.
CC -!- MASS SPECTROMETRY: Mass=30452; Method=Electrospray; Note=The measured
CC mass is that of mature SoxA with a diheme bound.;
CC Evidence={ECO:0000269|PubMed:10940005};
CC -!- SIMILARITY: Belongs to the SoxA family. {ECO:0000255}.
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DR EMBL; X79242; CAA55827.2; -; Genomic_DNA.
DR PIR; T46963; T46963.
DR RefSeq; WP_024845877.1; NZ_RIAQ01000020.1.
DR PDB; 2C1D; X-ray; 1.92 A; A/C/E/G=27-290.
DR PDBsum; 2C1D; -.
DR AlphaFoldDB; O33434; -.
DR SMR; O33434; -.
DR STRING; 935565.JAEM01000025_gene232; -.
DR KEGG; ag:CAA55827; -.
DR eggNOG; COG3258; Bacteria.
DR BioCyc; MetaCyc:SOXADENIT-MON; -.
DR BRENDA; 2.8.5.2; 4531.
DR EvolutionaryTrace; O33434; -.
DR GO; GO:0070069; C:cytochrome complex; IDA: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:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal 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:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0016783; F:sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0019417; P:sulfur oxidation; IDA: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.
DR PROSITE; PS51008; MULTIHEME_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; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:10940005"
FT CHAIN 27..290
FT /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT /evidence="ECO:0000269|PubMed:10940005"
FT /id="PRO_0000423488"
FT DOMAIN 78..171
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 251
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:16297640"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16297640"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16297640"
FT BINDING 106
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:16297640"
FT BINDING 109
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:16297640"
FT BINDING 110
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:16297640"
FT BINDING 143
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:16297640"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16297640"
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:16297640"
FT BINDING 209
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 210
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:16297640"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q939U1"
FT BINDING 251
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:16297640"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16297640"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2C1D"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2C1D"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:2C1D"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2C1D"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:2C1D"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2C1D"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:2C1D"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:2C1D"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2C1D"
SQ SEQUENCE 290 AA; 31748 MW; 28D4570C9390F909 CRC64;
MPRFTKTKGT LAATALGLAL AGAAFADPVE DGLVIETDSG PVEIVTKTAP PAFLADTFDT
IYSGWHFRDD STRDLERDDF DNPAMVFVDR GLDKWNAAMG VNGESCASCH QGPESMAGLR
AVMPRVDEHT GKLMIMEDYV NACVTERMGL EKWGVTSDNM KDMLSLISLQ SRGMAVNVKI
DGPAAPYWEH GKEIYYTRYG QLEMSCANCH EDNAGNMIRA DHLSQGQING FPTYRLKDSG
MVTAQHRFVG CVRDTRAETF KAGSDDFKAL ELYVASRGNG LSVEGVSVRH
