NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ismej.2007.46; PubMed=18059494 [NCBI, ExPASy, EBI, Israel, Japan]
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses.";
ISME J. 1:703-713(2007).

Comments

FUNCTION: Catalyzes the synthesis of activated sulfate.
CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3 .
SIMILARITY: Belongs to the APS kinase family.

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

CP000240; ABD02384.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_477647.1; -.

3D structure databases

ModBase

Q2JLM3.

Ontologies

GO:0004020;	Molecular function: adenylylsulfate kinase activity (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00065; -; 1.
PBIL [Tree]

InterPro

IPR002891; APS_kinase_C.
Graphical view of domain structure.

Pfam

PF01583; APS_kinase; 1.
Pfam graphical view of domain structure.

ProDom

PD002350; APS_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00455; apsK; 1.

ProtoNet

Q2JLM3.

Genome annotation databases

GeneID

3901321; -.

GenomeReviews

CP000240_GR; CYB_1417.

KEGG

cyb:CYB_1417; -.

TIGR

CYB_1417; -.

Phylogenomic databases

HOGENOM

Q2JLM3; -.

Other

UniRef

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

Keywords

ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 175`	`175`	`Adenylyl-sulfate kinase.`	`PRO_1000057447`
`NP_BIND`	`12 19`	`8`	`ATP (By similarity).`
`ACT_SITE`	`86 86`		`Phosphoserine intermediate (By similarity).`

Sequence information

Length: 175 AA [This is the length of the unprocessed precursor]

Molecular weight: 19543 Da [This is the MW of the unprocessed precursor]

CRC64: 024F60FBD64E8CD4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRRGVTVWF TGLSGAGKTT LSCGVAQQLR AWGLPVEVLD GDLVRQHLTK GLGFSKVDRE 

        70         80         90        100        110        120 
ENIRRIGFVA EMLTRHGVIV LVSAISPYRA ARQEVRRYIG SFIEVFVDAP LEVCERRDVK 

       130        140        150        160        170 
GLYRKARAGL IQHFTGIDDP YEPPEQPEVV CKTAEQSIPE CIDLVIQSLK SRGYV

Q2JLM3 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