[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5. STRAIN=K12; PubMed=1316900 [NCBI, ExPASy, EBI, Israel, Japan] Leyh T.S., Vogt T.F., Suo Y.; "The DNA sequence of the sulfate activation locus from Escherichia coli K-12."; J. Biol. Chem. 267:10405-10410(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. STRAIN=K12; DOI=10.1016/0378-1119(90)90504-K; PubMed=2185135 [NCBI, ExPASy, EBI, Israel, Japan] Malo M.S., Loughlin R.E.; "Promoter elements and regulation of expression of the cysD gene of Escherichia coli K-12."; Gene 87:127-131(1990).
[5]	CHARACTERIZATION. PubMed=2828368 [NCBI, ExPASy, EBI, Israel, Japan] Leyh T.S., Taylor J.C., Markham G.D.; "The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization."; J. Biol. Chem. 263:2409-2416(1988).

Comments

CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl sulfate.
ENZYME REGULATION: Stimulated by an intrinsic GTPase (Probably cysN).
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3 .
SUBUNIT: Heterodimer composed of cysD, the smaller subunit, and cysN.
SIMILARITY: Belongs to the PAPS reductase family. CysD 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

M74586; AAA23645.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U29579; AAA69262.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75794.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76829.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M35098; AAA74892.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D65056; D65056.

RefSeq

AP_003319.1; -.
NP_417232.1; -.

3D structure databases

SMR

P21156; 5-212.

ModBase

P21156.

Protein-protein interaction databases

DIP

DIP:360N; -.
DIP:9376N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:CYSD-MON; -.
MetaCyc:CYSD-MON; -.

2D gel databases

ECO2DBASE

H036.0; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0183; -.

EcoGene

EG10186; cysD.

Ontologies

GO:0004781;	Molecular function: sulfate adenylyltransferase (ATP) activity (inferred from electronic annotation from HAMAP).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
GO:0019421;	Biological process: sulfate reduction, APS pathway (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00064; -; 1.
PBIL [Tree]

InterPro

IPR011784; CysDAde_trans.
IPR002500; PAPS_reduct.
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.

PIRSF

PIRSF002936; CysDAde_trans; 1.

TIGRFAMs

TIGR02039; CysD; 1.

ProtoNet

P21156.

Genome annotation databases

GeneID

947217; -.

GenomeReviews

U00096_GR; b2752.
AP009048_GR; JW2722.

KEGG

ecj:JW2722; -.
eco:b2752; -.

Phylogenomic databases

HOGENOM

P21156; -.

Genome annotation databases

CMR

P21156; b2752.

Other

UniRef

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

Keywords

Complete proteome; Direct protein sequencing; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 302`	`302`	`Sulfate adenylyltransferase subunit 2.`	`PRO_0000100664`
`CONFLICT`	`180 180`		`S -> T (in Ref. 1; AAA23645).`

Sequence information

Length: 302 AA [This is the length of the unprocessed precursor]

Molecular weight: 35188 Da [This is the MW of the unprocessed precursor]

CRC64: A48881C0E5E086A1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQIRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA FYPGTLPFPL 

        70         80         90        100        110        120 
LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK 

       130        140        150        160        170        180 
QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES 

       190        200        210        220        230        240 
IRVFPLSNWT EQDIWQYIWL ENIDIVPLYL AAERPVLERD GMLMMIDDNR IDLQPGEVIK 

       250        260        270        280        290        300 
KRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG 


YF

P21156 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