CYSH_ALLVD
ID CYSH_ALLVD Reviewed; 256 AA.
AC D3RNJ4; Q9L9V0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, 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:10939523};
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: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:10939523};
GN OrderedLocusNames=Alvin_2447 {ECO:0000312|EMBL:ADC63359.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=10939523; DOI=10.1023/a:1007058421714;
RA Neumann S., Wynen A., Truper H.G., Dahl C.;
RT "Characterization of the cys gene locus from Allochromatium vinosum
RT indicates an unusual sulfate assimilation pathway.";
RL Mol. Biol. Rep. 27:27-33(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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 ECO:0000305|PubMed:10939523}.
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}.
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; AF163765; AAF27544.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63359.1; -; Genomic_DNA.
DR RefSeq; WP_012971629.1; NC_013851.1.
DR AlphaFoldDB; D3RNJ4; -.
DR SMR; D3RNJ4; -.
DR STRING; 572477.Alvin_2447; -.
DR EnsemblBacteria; ADC63359; ADC63359; Alvin_2447.
DR KEGG; alv:Alvin_2447; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_044089_1_0_6; -.
DR OMA; KTECGLW; -.
DR OrthoDB; 674332at2; -.
DR BioCyc; MetaCyc:MON-18530; -.
DR BRENDA; 1.8.4.10; 257.
DR Proteomes; UP000001441; 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.
DR TIGRFAMs; TIGR00434; cysH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..256
FT /note="Adenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000452767"
FT ACT_SITE 231
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
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 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 203
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 206
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ SEQUENCE 256 AA; 29144 MW; D5ABF1271E797C95 CRC64;
MTERRQPSLS TDTLPTREAA AIELLSQVCR ELDSIVFATS LGAEDMVLTE IIRRERLPIR
IFTLDTGRLP TETLELIEVV ERHYGTRIER YAPHPDAIAD YVSRYGLDGF YDSVPARQAC
CRVRKLEPLK RALAGQSAWV TGLRAEQSVT RAELPAREWD AANGLEKINP LADWSEHEVW
AFIRHHRVPY NPLHNQGYPS IGCAPCTRAI TVGEDVRAGR WWWENPETKE CGLHRREFAP
RQPSAHPAIE RDRSAA
