ID F7RL20_9GAMM Unreviewed; 260 AA.
AC F7RL20;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=SOHN41_00722 {ECO:0000313|EMBL:EGM70988.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM70988.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM70988.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM70988.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
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:EGM70988.1}.
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DR EMBL; AFOZ01000014; EGM70988.1; -; Genomic_DNA.
DR RefSeq; WP_007645612.1; NZ_AFOZ01000014.1.
DR AlphaFoldDB; F7RL20; -.
DR STRING; 327275.SOHN41_00722; -.
DR OrthoDB; 9794018at2; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000002956; 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 63..235
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT ACT_SITE 254
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ SEQUENCE 260 AA; 29307 MW; D6536E52057FF002 CRC64;
MADLEQKNSD AVPTVVSTAE LTALLSAPKA EQAIELERIN QFLAGLSAQE RVLWGLTYLP
GNHALSSSFG IQAAVMLHMV SQAQANIPVI LTDTGYLFPE TYQFIDELTE RLSLNLKVYQ
AAMTSAWQEA RFGKLWEQGL DGLEQYNRLN KVEPMQRALA ELEVGTWFAG LRRSQASTRE
ALPILAIHGT RFKLLPIIEW SNKDVHLYLT QFDLPYHPLW DQGYVSVGDT HSSKPLELGM
TEEETRFNGL KRECGLHYEI
//
