NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gr.4106106; PubMed=16365377 [NCBI, ExPASy, EBI, Israel, Japan]
Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.;
"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
Genome Res. 16:149-156(2006).

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

AP008232; BAE73793.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_454198.1; -.

3D structure databases

SMR

Q2NVN2; 2-230.

ModBase

Q2NVN2.

Enzyme and pathway databases

BioCyc

SGLO343509:SG0518-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

Q2NVN2.

Genome annotation databases

3868219; -.

AP008232_GR; SG0518.

sgl:SG0518; -.

fig|343509.6.peg.1173; -.

Phylogenomic databases

HOGENOM

Q2NVN2; -.

Genome annotation databases

CMR

Q2NVN2; SG0518.

Other

ProtoNet

Q2NVN2.

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`	`1 244`	`244`		`Phosphoadenosine phosphosulfate reductase.`	`PRO_1000008940`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 27701 Da [This is the MW of the unprocessed precursor]

CRC64: 6D744EBCB80A3900 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDWDLGELN ALEKAQQTAA LAAVNQQLES QTAEQRVAWA LEHLPEQAVL SSSFGIQAAV 

        70         80         90        100        110        120 
SLRLVTRQRP DIPVILTDTG YLFPETYRFI DELTETLGLN LQIFRATTSP AWQEARYGKL 

       130        140        150        160        170        180 
WEQGVEGIER YNQLNKVEPM NRALATLGAG TWFAGLRREQ SGSRAHLPVL AIQRGVFKLL 

       190        200        210        220        230        240 
PIIDWDNRQV YQYLTRHGLS YHPLWEQGYL SVGDTHTTRK CEPGMSEEET RFFGLKRECG 


LHEG

Q2NVN2 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