Reviewed, UniProtKB/Swiss-Prot P94498 (CYSH1_BACSU)

Names and origin

Protein names

Recommended name:
    Phosphoadenosine phosphosulfate reductase
    EC=1.8.4.8
Alternative name(s):
    PAPS reductase, thioredoxin dependent
    PAdoPS reductase
    3'-phosphoadenylylsulfate reductase
    PAPS sulfotransferase

Gene names

Name:	cysH
Ordered Locus Names:	BSU15570

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Reduction of activated sulfate into sulfite. HAMAP MF_00063
Catalytic activity	Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. HAMAP MF_00063
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3. HAMAP MF_00063
Subcellular location	Cytoplasm By similarity.
Induction	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.
Sequence similarities	Belongs to the PAPS reductase family. CysH subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphoadenylyl-sulfate reductase (thioredoxin) activity Inferred from electronic annotation. Source: HAMAP transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 233	233	Phosphoadenosine phosphosulfate reductase HAMAP MF_00063		PRO_0000100626
Experimental info
	Sequence conflict	134 – 141	8	SGHPAWLS → QDISLAF in AAC44833. Ref.1
	Sequence conflict	171 – 174	4	LIHW → HYPL in AAC44833. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P94498-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: F7A138D7D7583D45	FASTA	233	26,975
	10 20 30 40 50 60 MLTYDNWEEP TITFPEDDPY KGALSVLKWA YGHYGDQLVY ACSFGIEGIV LIDLIYKVKK 70 80 90 100 110 120 DAEIVFLDTG LHFKETYETI ERVKERYPGL NIILKKPDLT LEEQAEEHGD KLWEREPNQC 130 140 150 160 170 180 CYLRKVVPLR EALSGHPAWL SGLRRDQGPS RANTNFLNKD EKFKSVKVCP LIHWTWKDIW 190 200 210 220 230 RYTSRNELDY NPLHDQGYPS IGCAPCTSPA FTAEDLRSGR WNGMAKTECG LHE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9006060] [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: 9384377] [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: 11004190] [Abstract] Cited for: INDUCTION. Strain: 168 / JH642.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U76751 Genomic DNA. Translation: AAC44833.1. AJ000974 Genomic DNA. Translation: CAA04409.1. AL009126 Genomic DNA. Translation: CAB13431.1.
PIR	H69611.
RefSeq	NP_389440.1.
3D structure databases
HSSP	HSSP built from PDB template 1SUR based on UniProtKB P17854.
ModBase	Search...
Genome annotation databases
GeneID	938645.
GenomeReviews	Gene locus BSU15570 in contig AL009126_GR.
KEGG	bsu:BSU15570.
NMPDR	fig|224308.1.peg.1559.
Organism-specific databases
SubtiList	BG11930. cysH. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P94498.
OMA	P94498. FEETLAY.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1559-MON.
BRENDA	1.8.4.8. 150.
Family and domain databases
HAMAP	MF_00063. [Tree]
InterPro	IPR011798. APS_reductase. IPR004511. PAdo_PSO4_Rdtase_CysH. IPR002500. PAPS_reduct. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF01507. PAPS_reduct. 1 hit. [Graphical view]
TIGRFAMs	TIGR02055. APS_reductase. 1 hit. TIGR00434. cysH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CYSH1_BACSU

Accession

Primary (citable) accession number: P94498
Secondary accession number(s): O34620

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 30, 2000
Last modified:	June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)