CYSH_BURCE
ID CYSH_BURCE Reviewed; 250 AA.
AC Q9RFS6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE Short=APS reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:10613872};
DE EC=1.8.4.10 {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:10613872};
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:10613872};
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29424 / DBO1;
RX PubMed=10613872; DOI=10.1128/jb.182.1.135-142.2000;
RA Bick J.A., Dennis J.J., Zylstra G.J., Nowack J., Leustek T.;
RT "Identification of a new class of 5'-adenylylsulfate (APS) reductases from
RT sulfate-assimilating bacteria.";
RL J. Bacteriol. 182:135-142(2000).
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}.
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 -!- 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, ECO:0000305}.
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DR EMBL; AF170343; AAD50979.1; -; Genomic_DNA.
DR RefSeq; WP_006484803.1; NZ_KN150986.1.
DR AlphaFoldDB; Q9RFS6; -.
DR SMR; Q9RFS6; -.
DR STRING; 292.DM42_2595; -.
DR GeneID; 56559060; -.
DR KEGG; ag:AAD50979; -.
DR eggNOG; COG0175; Bacteria.
DR BRENDA; 1.8.4.10; 1028.
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 3: Inferred from homology;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT CHAIN 1..250
FT /note="Adenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000424294"
FT ACT_SITE 230
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ SEQUENCE 250 AA; 27881 MW; 9E0E7F8001A4A5D9 CRC64;
MSTATATALT PELAAKVERL DALLAQIGER HDKVKFASSL AAEDMLLTHA ILSKGVPIGI
FSLNTGRLHA ETLGMIDRVR ERYGYEIEQF HPQQDAVDRY VAEHGLNAFY ESVELRKSCC
HIRKVEPLNR ALADVGAWVT GQRREQSVTR AELHEEEQDE ARGIAKYNPL ADWTEADVWA
YLKAFDVPVN PLHARGYPSI GCEPCTRAIR PGEDSRAGRW WWESRDTKEC GLHITTITPI
PANAEAGAAH
