[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.; "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."; Jpn. Agric. Res. Q. 39:275-287(2005).

Comments

FUNCTION: Reduction of activated sulfate into sulfite.
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: Cytoplasm (By similarity).
SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AP008229; BAE69956.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_452230.1; -.

3D structure databases

ModBase

Q2P0H1.

Enzyme and pathway databases

BioCyc

XORY342109:XOO3201-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004604;	Molecular function: phosphoadenylyl-sulfate reductase (thioredoxin) activity (inferred from electronic annotation from HAMAP).
GO:0016740;	Molecular function: transferase activity (inferred from electronic annotation from InterPro).
GO:0019344;	Biological process: cysteine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019379;	Biological process: sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00063; -; 1.
PBIL [Tree]

InterPro

IPR004511; CysH.
IPR002500; PAPS_reduct.
IPR011800; PAPS_reductase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.

Pfam

PF01507; PAPS_reduct; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00434; cysH; 1.
TIGR02057; PAPS_reductase; 1.

ProtoNet

Q2P0H1.

Genome annotation databases

GeneID

3856489; -.

GenomeReviews

AP008229_GR; XOO3201.

KEGG

xom:XOO_3201; -.

Phylogenomic databases

HOGENOM

Q2P0H1; -.

Genome annotation databases

CMR

Q2P0H1; XOO3201.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 241`	`241`		`Phosphoadenosine phosphosulfate reductase.`	`PRO_1000008946`

Sequence information

Length: 241 AA [This is the length of the unprocessed precursor]

Molecular weight: 27660 Da [This is the MW of the unprocessed precursor]

CRC64: 94931F3293593392 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTALPAASIT SSALDDLDAL NAQLEGLRAD ERVAWALQHG PQDAALSSSF GAQSAVTLHL 

        70         80         90        100        110        120 
LSQQRPDIPV ILIDTGYLFP ETYRFADALT ERLKLNLKVY RPLVSRAWME ARHGRLWEQG 

       130        140        150        160        170        180 
MVGIDQYNNL RKVEPMRRAL DELNVGTWFT GLRRSQSGGR AQTPIVQKRG ERYKISPIAD 

       190        200        210        220        230        240 
WTDRDVWQYL QAHELPYHPL WEQGYVSIGD FHTTRRWEPG MREEDTRFFG LKRECGIHED 


I

Q2P0H1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools