CYSH_VIBVU
ID CYSH_VIBVU Reviewed; 258 AA.
AC Q8CWK6;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE Short=PAPS reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE EC=1.8.4.8 {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=PAPS sulfotransferase {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=PAdoPS reductase {ECO:0000255|HAMAP-Rule:MF_00063};
GN Name=cysH {ECO:0000255|HAMAP-Rule:MF_00063}; OrderedLocusNames=VV1_1404;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'-
CC phosphosulfate (PAPS) using thioredoxin as an electron donor.
CC {ECO:0000255|HAMAP-Rule:MF_00063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2
CC H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol;
CC Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00063};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00063}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00063}.
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DR EMBL; AE016795; AAO09853.1; -; Genomic_DNA.
DR RefSeq; WP_011079378.1; NC_004459.3.
DR PDB; 6VPU; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-258.
DR PDBsum; 6VPU; -.
DR AlphaFoldDB; Q8CWK6; -.
DR SMR; Q8CWK6; -.
DR EnsemblBacteria; AAO09853; AAO09853; VV1_1404.
DR KEGG; vvu:VV1_1404; -.
DR HOGENOM; CLU_044089_3_0_6; -.
DR OMA; PIARWTQ; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-UniRule.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR011800; PAPS_reductase_CysH.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF000857; PAPS_reductase; 1.
DR TIGRFAMs; TIGR00434; cysH; 1.
DR TIGRFAMs; TIGR02057; PAPS_reductase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Oxidoreductase.
FT CHAIN 1..258
FT /note="Phosphoadenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000100654"
FT ACT_SITE 244
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:6VPU"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6VPU"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:6VPU"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:6VPU"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:6VPU"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6VPU"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6VPU"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6VPU"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:6VPU"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6VPU"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6VPU"
SQ SEQUENCE 258 AA; 29448 MW; C5078F647D681687 CRC64;
MLDSVASTLQ LSELLSLTKA EQSIRLAEIN VELEMLSAQE RVAWALQNLE GAHAVSSSFG
IQAAVMLHLV SKQQADIPVI LTDTGYLFPE TYQFIDELTK SLNLNLKVYR ANESANWQEA
RYGKLWEQGI EGIEKYNKLN KVEPMRRALN ELNVKTWFSG LRREQSQSRA GLPILSIQNG
VFKFLPVVDW SNKDVHYYLK EHGLSYHPLW EQGYLSVGDT HTTQKWEPGM SEEETRFFGL
KRECGLHEED NEQDGSGI
