CYSH_SINF2
ID CYSH_SINF2 Reviewed; 251 AA.
AC I3X057;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:10464198};
DE Short=APS reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:10464198};
DE EC=1.8.4.10 {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:10464198};
DE AltName: Full=5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305};
DE AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305};
GN Name=cysH {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:10464198};
GN ORFNames=USDA257_c06700 {ECO:0000312|EMBL:AFL49263.1};
OS Sinorhizobium fredii (strain USDA 257).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1185652;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA 257;
RX PubMed=22843606; DOI=10.1128/jb.00966-12;
RA Schuldes J., Rodriguez Orbegoso M., Schmeisser C., Krishnan H.B.,
RA Daniel R., Streit W.R.;
RT "Complete genome sequence of the broad-host-range strain Sinorhizobium
RT fredii USDA257.";
RL J. Bacteriol. 194:4483-4483(2012).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=USDA 257;
RX PubMed=10464198; DOI=10.1128/jb.181.17.5280-5287.1999;
RA Abola A.P., Willits M.G., Wang R.C., Long S.R.;
RT "Reduction of adenosine-5'-phosphosulfate instead of 3'-phosphoadenosine-
RT 5'-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other
RT members of the family Rhizobiaceae.";
RL J. Bacteriol. 181:5280-5287(1999).
CC -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC phosphosulfate (APS) using thioredoxin as an electron donor.
CC {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:10464198}.
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:0000255|HAMAP-Rule:MF_00063,
CC ECO:0000269|PubMed:10464198};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00063};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00063};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003563; AFL49263.1; -; Genomic_DNA.
DR RefSeq; WP_014761454.1; NC_018000.1.
DR AlphaFoldDB; I3X057; -.
DR SMR; I3X057; -.
DR STRING; 1185652.USDA257_c06700; -.
DR EnsemblBacteria; AFL49263; AFL49263; USDA257_c06700.
DR KEGG; sfd:USDA257_c06700; -.
DR PATRIC; fig|1185652.3.peg.693; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_044089_1_0_5; -.
DR Proteomes; UP000006180; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR011798; APS_reductase.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF000857; PAPS_reductase; 1.
DR TIGRFAMs; TIGR02055; APS_reductase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT ACT_SITE 232
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ SEQUENCE 251 AA; 27443 MW; 2B0150877C3EFAEF CRC64;
MTTQSLEAEA KALNDKLESL DLAGRLAMVA GLDGRAVFTT SLGIEDQVIT AAIGINRLDI
EVATLKTGRL FNETVALVEE TEETYNILIK RYYPEKADIE AYVAQYGMNG FYESVEARHA
CCGVRKLKPL ARALEGASYW ITGLRRGQSG NRATTPFAEA DLERGLIKIN PLADWDIETI
RAHVAAEAIP VNPLHGRGYP SIGCEPCTRA IKPGEPERAG RWWWENDEKR ECGLHVAEAA
SSIIPNASSA A
