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Protein

Phosphoadenosine phosphosulfate reductase

Gene

cysH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Reduction of activated sulfate into sulfite.

Catalytic activityi

Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes sulfite from sulfate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Sulfate adenylyltransferase (sat), Probable sulfate adenylyltransferase (yitA)
  2. Probable adenylyl-sulfate kinase (cysC), Probable adenylyl-sulfate kinase (yisZ)
  3. Phosphoadenosine phosphosulfate reductase (cysH), Probable phosphoadenosine phosphosulfate reductase (yitB)
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfite from sulfate, the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciBSUB:BSU15570-MONOMER.
UniPathwayiUPA00140; UER00206.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoadenosine phosphosulfate reductase (EC:1.8.4.8)
Alternative name(s):
3'-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAPS sulfotransferase
PAdoPS reductase
Gene namesi
Name:cysH
Ordered Locus Names:BSU15570
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Phosphoadenosine phosphosulfate reductasePRO_0000100626Add
BLAST

Proteomic databases

PaxDbiP94498.

Expressioni

Inductioni

Up-regulated by sulfur starvation and repressed by cysteine. Also induced by O-acetyl-L-serine (OAS), a direct precursor of cysteine, maybe via inactivation of a putative transcriptional repressor of the cysH operon whose activity is controlled by the intracellular levels of OAS.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008606.

Structurei

3D structure databases

ProteinModelPortaliP94498.
SMRiP94498. Positions 21-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAPS reductase family. CysH subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105ET3. Bacteria.
COG0175. LUCA.
HOGENOMiHOG000249397.
InParanoidiP94498.
KOiK00390.
OMAiPLAAWTQ.
OrthoDBiEOG6V1M7D.
PhylomeDBiP94498.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00063. CysH.
InterProiIPR011798. APS_reductase.
IPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFiPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsiTIGR02055. APS_reductase. 1 hit.
TIGR00434. cysH. 1 hit.

Sequencei

Sequence statusi: Complete.

P94498-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTYDNWEEP TITFPEDDPY KGALSVLKWA YGHYGDQLVY ACSFGIEGIV
60 70 80 90 100
LIDLIYKVKK DAEIVFLDTG LHFKETYETI ERVKERYPGL NIILKKPDLT
110 120 130 140 150
LEEQAEEHGD KLWEREPNQC CYLRKVVPLR EALSGHPAWL SGLRRDQGPS
160 170 180 190 200
RANTNFLNKD EKFKSVKVCP LIHWTWKDIW RYTSRNELDY NPLHDQGYPS
210 220 230
IGCAPCTSPA FTAEDLRSGR WNGMAKTECG LHE
Length:233
Mass (Da):26,975
Last modified:May 30, 2000 - v2
Checksum:iF7A138D7D7583D45
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1418SGHPAWLS → QDISLAF in AAC44833 (PubMed:9006060).Curated
Sequence conflicti171 – 1744LIHW → HYPL in AAC44833 (PubMed:9006060).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76751 Genomic DNA. Translation: AAC44833.1.
AJ000974 Genomic DNA. Translation: CAA04409.1.
AL009126 Genomic DNA. Translation: CAB13431.1.
PIRiH69611.
RefSeqiNP_389440.1. NC_000964.3.
WP_003232103.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13431; CAB13431; BSU15570.
GeneIDi938645.
KEGGibsu:BSU15570.
PATRICi18974921. VBIBacSub10457_1652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76751 Genomic DNA. Translation: AAC44833.1.
AJ000974 Genomic DNA. Translation: CAA04409.1.
AL009126 Genomic DNA. Translation: CAB13431.1.
PIRiH69611.
RefSeqiNP_389440.1. NC_000964.3.
WP_003232103.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP94498.
SMRiP94498. Positions 21-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008606.

Proteomic databases

PaxDbiP94498.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13431; CAB13431; BSU15570.
GeneIDi938645.
KEGGibsu:BSU15570.
PATRICi18974921. VBIBacSub10457_1652.

Phylogenomic databases

eggNOGiENOG4105ET3. Bacteria.
COG0175. LUCA.
HOGENOMiHOG000249397.
InParanoidiP94498.
KOiK00390.
OMAiPLAAWTQ.
OrthoDBiEOG6V1M7D.
PhylomeDBiP94498.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00206.
BioCyciBSUB:BSU15570-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00063. CysH.
InterProiIPR011798. APS_reductase.
IPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFiPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsiTIGR02055. APS_reductase. 1 hit.
TIGR00434. cysH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase."
    Mansilla M.C., de Mendoza D.
    J. Bacteriol. 179:976-981(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of the pyr operon."
    Foulger D., Errington J.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis."
    Mansilla M.C., Albanesi D., de Mendoza D.
    J. Bacteriol. 182:5885-5892(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168 / JH642.

Entry informationi

Entry nameiCYSH1_BACSU
AccessioniPrimary (citable) accession number: P94498
Secondary accession number(s): O34620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: February 17, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.