[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00028905; PubMed=1463852 [NCBI, ExPASy, EBI, Israel, Japan] Niehaus A., Gisselmann G., Schwenn J.D.; "Primary structure of the Synechococcus PCC 7942 PAPS reductase gene."; Plant Mol. Biol. 20:1179-1183(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Holtman C.K., Socias T., Mohler B.J., Chen Y., Min H., Golden S.S., Youderian P., Sandoval P., Gonzalez A., Salinas I.; "Synechococcus elongatus PCC7942 genome sequence, cosmid 7H1 and 2E8."; Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.; "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

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

M84476; AAA27328.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U30252; AAL03931.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000100; ABB58536.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S28609; S28609.

RefSeq

YP_401523.1; -.

3D structure databases

HSSP

P17854; 1SUR. [HSSP ENTRY / PDB]

ModBase

Q55309.

Enzyme and pathway databases

BioCyc

SELO1140:SYNPCC7942_2506-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: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.

BLOCKS

Q55309.

Genome annotation databases

GeneID

3774526; -.

GenomeReviews

CP000100_GR; Synpcc7942_2506.

KEGG

syf:Synpcc7942_2506; -.

Phylogenomic databases

HOGENOM

Q55309; -.

Genome annotation databases

CMR

Q55309; Synpcc7942_2506.

Other

ProtoNet

Q55309.

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`	`1 232`	`232`	`Phosphoadenosine phosphosulfate reductase.`	`PRO_0000100649`
`CONFLICT`	`218 218`		`S -> T (in Ref. 1; AAA27328).`

Sequence information

Length: 232 AA [This is the length of the unprocessed precursor]

Molecular weight: 26622 Da [This is the MW of the unprocessed precursor]

CRC64: 549FFECCB3BF89A6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPALLPSLTE INAQLADQAA TQIIQWAATE FGSGLVLSTS FGIQSAVMLH LATQVQPDIP 

        70         80         90        100        110        120 
VIWIDTGYLP TETYRFAAEL TERLKLNLKV YQSEISPARM EALYGRLWES ESVEDFNRYD 

       130        140        150        160        170        180 
QMRKVEPMNR ALQELGATAW LSGVRRQQTA HRQSMEIVEL KRDRYAIRPI LGWHSRDVYQ 

       190        200        210        220        230 
YLTAHDLPYH PLFDQGYVTV GDWHSSRPLQ ADDSDERSTR FRGLKQECGL HL

Q55309 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