Reviewed, UniProtKB/Swiss-Prot A9N2E4 (CYSH_SALPB)

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:	SPAB_03655

Organism

Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]

Taxonomic identifier

272994 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella enterica subsp. enterica serovar Paratyphi B

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Reduction of activated sulfate into sulfite By similarity.
Catalytic activity	Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3.
Subcellular location	CytoplasmBy similarity.
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: HAMAP
Molecular function	phosphoadenylyl-sulfate reductase (thioredoxin) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 244	244	Phosphoadenosine phosphosulfate reductase		PRO_1000075075

Sequences

	Sequence		Length	Mass (Da)
	A9N2E4-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 3D4D8CEB2875C807	FASTA	244	27,996
	10 20 30 40 50 60 MSKLDLNALN ELPKVDRVLA LAETNAQLET LTAEERVAWA LENLPGEYVL SSSFGIQAAV 70 80 90 100 110 120 SLHLVNQIRP DIPVILTDTG YLFPETYQFI DELTDKLKLN LKVYRAGESP AWQEARYGKL 130 140 150 160 170 180 WEQGVEGIEK YNEINKVEPM NRALKELKAQ TWFAGLRREQ SGSRAHLPVL AIQRGVFKVL 190 200 210 220 230 240 PIIDWDNRTV YQYLQKHGLK YHPLWDQGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG

References

[1]	McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000886 Genomic DNA. Translation: ABX68995.1.
RefSeq	YP_001589828.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5778103.
GenomeReviews	Gene locus SPAB_03655 in contig CP000886_GR.
KEGG	spq:SPAB_03655.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00063. [Tree]
InterPro	IPR004511. CysH. IPR011800. PAPS_reductase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
TIGRFAMs	TIGR00434. cysH. 1 hit. TIGR02057. PAPS_reductase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CYSH_SALPB

Accession

Primary (citable) accession number: A9N2E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	November 25, 2008
This is version 10 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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