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Database: UniProt
Entry: A0A0B8P004_9VIBR
LinkDB: A0A0B8P004_9VIBR
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ID   A0A0B8P004_9VIBR        Unreviewed;       214 AA.
AC   A0A0B8P004;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            Short=PAPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.8 {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS sulfotransferase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAdoPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063};
GN   ORFNames=JCM19231_2442 {ECO:0000313|EMBL:GAM56633.1};
OS   Vibrio ishigakensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM56633.1, ECO:0000313|Proteomes:UP000031671};
RN   [1] {ECO:0000313|EMBL:GAM56633.1, ECO:0000313|Proteomes:UP000031671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA   Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT   "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAM56633.1, ECO:0000313|Proteomes:UP000031671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG   NBRP consortium;
RA   Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL   Submitted (JAN-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00063};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 3/3. {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|ARBA:ARBA00009732, ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAM56633.1}.
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DR   EMBL; BBRZ01000034; GAM56633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B8P004; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000031671; Unassembled WGS sequence.
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; HUPs; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 1.
DR   PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00063}; Reference proteome {ECO:0000313|Proteomes:UP000031671}.
FT   DOMAIN          10..181
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   ACT_SITE        201
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   214 AA;  24213 MW;  4371625258BEFE0D CRC64;
     MALENLQPNF ALSSSFGAQA AVMLHLVTRQ KPDVPVILTD TGYLFKETYQ FIDELTLLLD
     LNLKVYRSPI SPAWQESRFG QLWDKGVEGI TQYNQLNKVE PMRRALSDLN VGTWFSGLRR
     AQSDSRSGLP VLSIQHGVFK FLPILDWSDE KVETYIEEHA LPKHPLTAQG YVSIGDIHTT
     DKLEEGMKQQ DTRFFGLKRE CGLHEDTESD GSGI
//
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