THTR_AZOVI
ID THTR_AZOVI Reviewed; 271 AA.
AC P52197;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Thiosulfate sulfurtransferase;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese-like protein;
GN Name=rhdA;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RC STRAIN=OP / UW136;
RX PubMed=8617271; DOI=10.1111/j.1432-1033.1996.00240.x;
RA Colnaghi R., Pagani S., Kennedy C., Drummond M.;
RT "Cloning, sequence analysis and overexpression of the rhodanese gene of
RT Azotobacter vinelandii.";
RL Eur. J. Biochem. 236:240-248(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10788330; DOI=10.1006/jmbi.2000.3651;
RA Bordo D., Deriu D., Colnaghi R., Carpen A., Pagani S., Bolognesi M.;
RT "The crystal structure of a sulfurtransferase from Azotobacter vinelandii
RT highlights the evolutionary relationship between the rhodanese and
RT phosphatase enzyme families.";
RL J. Mol. Biol. 298:691-704(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=11592406; DOI=10.1515/bc.2001.155;
RA Bordo D., Forlani F., Spallarossa A., Colnaghi R., Carpen A., Bolognesi M.,
RA Pagani S.;
RT "A persulfurated cysteine promotes active site reactivity in Azotobacter
RT vinelandii Rhodanese.";
RL Biol. Chem. 382:1245-1252(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33542; EC=2.8.1.1;
CC -!- INTERACTION:
CC P52197; P0A6B7: iscS; Xeno; NbExp=2; IntAct=EBI-7906952, EBI-550055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
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DR EMBL; L42346; AAB03239.1; -; Genomic_DNA.
DR PIR; S62187; S62187.
DR RefSeq; WP_012699416.1; NZ_FPKM01000008.1.
DR PDB; 1E0C; X-ray; 1.80 A; A=1-271.
DR PDB; 1H4K; X-ray; 2.05 A; X=1-271.
DR PDB; 1H4M; X-ray; 2.10 A; X=1-271.
DR PDBsum; 1E0C; -.
DR PDBsum; 1H4K; -.
DR PDBsum; 1H4M; -.
DR AlphaFoldDB; P52197; -.
DR BMRB; P52197; -.
DR SMR; P52197; -.
DR IntAct; P52197; 1.
DR MINT; P52197; -.
DR DrugBank; DB04053; Hypophosphite.
DR OMA; GYPRVKG; -.
DR BioCyc; MetaCyc:MON-12548; -.
DR BRENDA; 2.8.1.1; 49.
DR EvolutionaryTrace; P52197; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Repeat; Transferase.
FT CHAIN 1..271
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000139406"
FT DOMAIN 21..129
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 159..270
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 230
FT /note="Cysteine persulfide intermediate"
FT BINDING 235
FT /ligand="substrate"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:1E0C"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:1E0C"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1E0C"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:1E0C"
SQ SEQUENCE 271 AA; 29629 MW; 47E573D2D34EA77C CRC64;
MDDFASLPLV IEPADLQARL SAPELILVDL TSAARYAEGH IPGARFVDPK RTQLGQPPAP
GLQPPREQLE SLFGELGHRP EAVYVVYDDE GGGWAGRFIW LLDVIGQQRY HYLNGGLTAW
LAEDRPLSRE LPAPAGGPVA LSLHDEPTAS RDYLLGRLGA ADLAIWDARS PQEYRGEKVL
AAKGGHIPGA VNFEWTAAMD PSRALRIRTD IAGRLEELGI TPDKEIVTHC QTHHRSGLTY
LIAKALGYPR VKGYAGSWGE WGNHPDTPVE L
