ID W4SFR8_9XANT Unreviewed; 241 AA.
AC W4SFR8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ECO:0000313|EMBL:GAE55242.1};
GN ORFNames=XPR_1877 {ECO:0000313|EMBL:GAE55242.1};
OS Xanthomonas arboricola pv. pruni MAFF 301420.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1418095 {ECO:0000313|EMBL:GAE55242.1, ECO:0000313|Proteomes:UP000019084};
RN [1] {ECO:0000313|EMBL:GAE55242.1, ECO:0000313|Proteomes:UP000019084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 301420 {ECO:0000313|Proteomes:UP000019084};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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:GAE55242.1}.
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DR EMBL; BAVC01000142; GAE55242.1; -; Genomic_DNA.
DR AlphaFoldDB; W4SFR8; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000019084; 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; IPR011800; PAPS_reductase_CysH.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00434; cysH; 1.
DR NCBIfam; TIGR02057; PAPS_reductase; 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}.
FT DOMAIN 44..215
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT ACT_SITE 235
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ SEQUENCE 241 AA; 27600 MW; 97EA544CF505C4B2 CRC64;
MTALPAASIT ASALDDLDAL NAQLEGLRAD ERVAWALQHG PQEAALSSSF GAQSAVTLHL
LTQQRPDIPV ILIDTGYLFP ETYRFADALA DRLKLNLKVY RPLVSRAWME ARHGRLWEQG
MVGIDQYNNL RKVEPMRRAL DELNVGTWFT GLRRSQSGGR AQTPIVQKRG ERYKVSPIAD
WTDRDVWQYL QAHDLPYHPL WEQGYVSIGD FHTTRRWEPG MREEDTRFFG LKRECGIHED
I
//
