CYSH1_BACSU
ID CYSH1_BACSU Reviewed; 233 AA.
AC P94498; O34620;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Adenosine 5'-phosphosulfate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00063};
DE Short=APS reductase 1 {ECO:0000255|HAMAP-Rule:MF_00063};
DE EC=1.8.4.10 {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:12072441};
DE AltName: Full=5'-adenylylsulfate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00063};
GN Name=cysH; OrderedLocusNames=BSU15570;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9006060; DOI=10.1128/jb.179.3.976-981.1997;
RA Mansilla M.C., de Mendoza D.;
RT "L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing,
RT and functional characterization of the gene coding for
RT phosphoadenylylsulfate sulfotransferase.";
RL J. Bacteriol. 179:976-981(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Foulger D., Errington J.;
RT "Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of
RT the pyr operon.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION.
RC STRAIN=168 / JH642;
RX PubMed=11004190; DOI=10.1128/jb.182.20.5885-5892.2000;
RA Mansilla M.C., Albanesi D., de Mendoza D.;
RT "Transcriptional control of the sulfur-regulated cysH operon, containing
RT genes involved in L-cysteine biosynthesis in Bacillus subtilis.";
RL J. Bacteriol. 182:5885-5892(2000).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12072441; DOI=10.1074/jbc.m204613200;
RA Williams S.J., Senaratne R.H., Mougous J.D., Riley L.W., Bertozzi C.R.;
RT "5'-adenosinephosphosulfate lies at a metabolic branch point in
RT mycobacteria.";
RL J. Biol. Chem. 277:32606-32615(2002).
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:12072441}.
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:12072441};
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 -!- INDUCTION: Up-regulated by sulfur starvation and repressed by cysteine.
CC Also induced by O-acetyl-L-serine (OAS), a direct precursor of
CC cysteine, maybe via inactivation of a putative transcriptional
CC repressor of the cysH operon whose activity is controlled by the
CC intracellular levels of OAS. {ECO:0000269|PubMed:11004190}.
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; U76751; AAC44833.1; -; Genomic_DNA.
DR EMBL; AJ000974; CAA04409.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13431.1; -; Genomic_DNA.
DR PIR; H69611; H69611.
DR RefSeq; NP_389440.1; NC_000964.3.
DR RefSeq; WP_003232103.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P94498; -.
DR SMR; P94498; -.
DR STRING; 224308.BSU15570; -.
DR PaxDb; P94498; -.
DR PRIDE; P94498; -.
DR EnsemblBacteria; CAB13431; CAB13431; BSU_15570.
DR GeneID; 938645; -.
DR KEGG; bsu:BSU15570; -.
DR PATRIC; fig|224308.179.peg.1697; -.
DR eggNOG; COG0175; Bacteria.
DR InParanoid; P94498; -.
DR OMA; PIARWTQ; -.
DR PhylomeDB; P94498; -.
DR BioCyc; BSUB:BSU15570-MON; -.
DR Proteomes; UP000001570; Chromosome.
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:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IBA:GO_Central.
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); IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..233
FT /note="Adenosine 5'-phosphosulfate reductase 1"
FT /id="PRO_0000100626"
FT ACT_SITE 229
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"
FT CONFLICT 134..141
FT /note="SGHPAWLS -> QDISLAF (in Ref. 1; AAC44833)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..174
FT /note="LIHW -> HYPL (in Ref. 1; AAC44833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 26975 MW; F7A138D7D7583D45 CRC64;
MLTYDNWEEP TITFPEDDPY KGALSVLKWA YGHYGDQLVY ACSFGIEGIV LIDLIYKVKK
DAEIVFLDTG LHFKETYETI ERVKERYPGL NIILKKPDLT LEEQAEEHGD KLWEREPNQC
CYLRKVVPLR EALSGHPAWL SGLRRDQGPS RANTNFLNKD EKFKSVKVCP LIHWTWKDIW
RYTSRNELDY NPLHDQGYPS IGCAPCTSPA FTAEDLRSGR WNGMAKTECG LHE
