Q81T49 (CYSH_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	cysH
Ordered Locus Names:	BA_1440, GBAA_1440, BAS1330

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 HAMAP MF_00063.
Sequence similarities	Belongs to the PAPS reductase family. CysH subfamily.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 226	226	Phosphoadenosine phosphosulfate reductase HAMAP MF_00063		PRO_0000100623

Sequences

	Sequence		Length	Mass (Da)
	Q81T49 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3FF2A81C8BCA282A	FASTA	226	26,393
	10 20 30 40 50 60 MLTYETWEEN ETKGALSVLS WAYKEYKSEI VYACSFGVEG MVLLDLINQV NPSAKVVFLD 70 80 90 100 110 120 TNVHFQETYE LIQKVRERFP SLNIIEKQPK LTLDEQDKLH GDKLWESNPN LCCKIRKILP 130 140 150 160 170 180 LEESLANEKA WISGLRREQS ETRKHTKFIN QDHRFQSIKV CPLIHWTWKE VWRYVYKHSL 190 200 210 220 PYNSLHDIGY PSIGCEKCTL PVGEGGDSRD GRWAGKVKTE CGLHYQ

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP25382.1. AE017334 Genomic DNA. Translation: AAT30539.1. AE017225 Genomic DNA. Translation: AAT53650.1.
RefSeq	NP_843896.1. NC_003997.3. YP_018064.1. NC_007530.2. YP_027599.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81T49.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000011853; EBBACP00000011609; EBBACG00000011845. EBBACT00000017899; EBBACP00000017520; EBBACG00000017890. EBBACT00000022609; EBBACP00000022094; EBBACG00000022600.
GeneID	1086013. 2816195. 2849690.
GenomeReviews	Gene locus BA_1440 in contig AE016879_GR. Gene locus BAS1330 in contig AE017225_GR. Gene locus GBAA_1440 in contig AE017334_GR.
KEGG	ban:BA_1440. bar:GBAA_1440. bat:BAS1330.
TIGR	BA_1440. GBAA_1440.
Phylogenomic databases
GeneTree	EBGT00050000002870.
HOGENOM	HBG758022.
OMA	AIHGTRF.
ProtClustDB	CLSK916236.
Enzyme and pathway databases
BioCyc	BANT260799:BAS1330-MONOMER. BANT261594:GBAA1440-MONOMER.
Family and domain databases
HAMAP	MF_00063. CysH. [Tree]
InterPro	IPR011798. APS_reductase. IPR004511. PAPS/APS_Rdtase. 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.
KO	K00390.
Pfam	PF01507. PAPS_reduct. 1 hit. [Graphical view]
PIRSF	PIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMs	TIGR02055. APS_reductase. 1 hit. TIGR00434. CysH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CYSH_BACAN

Accession

Primary (citable) accession number: Q81T49
Secondary accession number(s): Q6I1D2, Q6KV78

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program