Reviewed, UniProtKB/Swiss-Prot Q8PHC7 (CYSH_XANAC)

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:	XAC3332

Organism

Xanthomonas axonopodis pv. citri (Citrus canker) [Complete proteome] [HAMAP]

Taxonomic identifier

92829 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	241 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. 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.
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 – 241	241	Phosphoadenosine phosphosulfate reductase HAMAP MF_00063		PRO_0000100656

Sequences

	Sequence		Length	Mass (Da)
	Q8PHC7-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 7FA3E68D2823FC22	FASTA	241	27,726
	10 20 30 40 50 60 MTALPAASIT SSAFDDLDAL NAQLEGLRAD QRVAWALQHG PQNAALSSSF GAQSAVTLHL 70 80 90 100 110 120 LSQQRPDIPV ILIDTGYLFP ETYRFADALT ERLKLNLKVY RPLVSRAWME ARHGRLWEQG 130 140 150 160 170 180 MVGIDQYNNL RKVEPMRRAL NELDVGTWFT GLRRSQSGGR AQTPIMQKRG ERYKISPIAD 190 200 210 220 230 240 WTDRDVWQYL QAHDLPYHPL WEQGYVSIGD FHTTRRWEPG MREEDTRFYG LKRECGIHED I

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE011979 Genomic DNA. Translation: AAM38175.1.
RefSeq	NP_643639.1.
3D structure databases
HSSP	HSSP built from PDB template 1SUR based on UniProtKB P17854.
ModBase	Search...
Genome annotation databases
GeneID	1157403.
GenomeReviews	Gene locus XAC3332 in contig AE008923_GR.
KEGG	xac:XAC3332.
NMPDR	fig|190486.1.peg.3283.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8PHC7.
OMA	Q8PHC7. TRFNGLK.
Enzyme and pathway databases
BioCyc	XAXO190486:XAC3332-MON.
BRENDA	1.8.4.8. 289771.
Family and domain databases
HAMAP	MF_00063. [Tree]
InterPro	IPR004511. PAdo_PSO4_Rdtase_CysH. IPR002500. PAPS_reduct. 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.
Pfam	PF01507. PAPS_reduct. 1 hit. [Graphical view]
TIGRFAMs	TIGR00434. cysH. 1 hit. TIGR02057. PAPS_reductase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CYSH_XANAC

Accession

Primary (citable) accession number: Q8PHC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 44 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)