ID G6F1F9_9PROT Unreviewed; 252 AA.
AC G6F1F9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE Short=APS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE EC=1.8.4.10 {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=5'-adenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063};
GN ORFNames=CIN_14550 {ECO:0000313|EMBL:EHD13263.1};
OS Commensalibacter intestini A911.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD13263.1, ECO:0000313|Proteomes:UP000005939};
RN [1] {ECO:0000313|EMBL:EHD13263.1, ECO:0000313|Proteomes:UP000005939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A911 {ECO:0000313|EMBL:EHD13263.1,
RC ECO:0000313|Proteomes:UP000005939};
RA Lee W.-J., Kim E.-K.;
RT "Genome Sequence of Commensalibacter intestini A911, isolated from
RT Drosophila gut.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC phosphosulfate (APS) using thioredoxin as an electron donor.
CC {ECO:0000256|HAMAP-Rule:MF_00063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + AMP + 2 H(+) + sulfite =
CC [thioredoxin]-dithiol + adenosine 5'-phosphosulfate;
CC Xref=Rhea:RHEA:21976, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215;
CC EC=1.8.4.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00063};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00063};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00063};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate. {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: 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:EHD13263.1}.
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DR EMBL; AGFR01000009; EHD13263.1; -; Genomic_DNA.
DR RefSeq; WP_008854445.1; NZ_AGFR01000009.1.
DR AlphaFoldDB; G6F1F9; -.
DR STRING; 1088868.CIN_14550; -.
DR PATRIC; fig|1088868.3.peg.1464; -.
DR eggNOG; COG0175; Bacteria.
DR OrthoDB; 9794018at2; -.
DR Proteomes; UP000005939; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR46482:SF9; 5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR46482; 5'-ADENYLYLSULFATE REDUCTASE 3, CHLOROPLASTIC; 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 Iron {ECO:0000256|HAMAP-Rule:MF_00063};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00063};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00063}.
FT DOMAIN 36..214
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT ACT_SITE 236
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ SEQUENCE 252 AA; 29085 MW; 89DA8B6635F97304 CRC64;
MTPIELYSQR PSETYSQKLR ATEDLLKQVT QDYTSLVQAT SLGVEDMVIT DIIHRLKLPI
TISMLDTKRL HEQTVALKEH AENHYGITIH TYYPDDTKVK EYVEKNGLDG FYNSLELRKE
CCHIRKLVPL QALRHGHEGW LTGLRKEQSD FRANLQAIED ENPTDSTQPR VKINPVLDWT
IGDIWHYVKE NSVPYNPLHD QFFVSIGCEP CTRAIALGED FRAGRWWWEQ DGAKECGLHV
HEASSLSNRP SK
//
