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Q7NVN5 (CYSN_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfate adenylyltransferase subunit 1

EC=2.7.7.4
Alternative name(s):
ATP-sulfurylase large subunit
Sulfate adenylate transferase
Short name=SAT
Gene names
Name:cysN
Ordered Locus Names:CV_2307
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

May be the GTPase, regulating ATP sulfurylase activity By similarity. HAMAP-Rule MF_00062

Catalytic activity

ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP-Rule MF_00062

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. HAMAP-Rule MF_00062

Subunit structure

Heterodimer composed of CysD, the smaller subunit, and CysN By similarity.

Sequence similarities

Belongs to the GTP-binding elongation factor family. CysN/NodQ subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Sulfate adenylyltransferase subunit 1 HAMAP-Rule MF_00062
PRO_0000091521

Regions

Nucleotide binding31 – 388GTP By similarity
Nucleotide binding110 – 1145GTP By similarity
Nucleotide binding165 – 1684GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NVN5 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 2256306774D4BE87

FASTA47752,841
        10         20         30         40         50         60 
MSHQSELIAG DILEYLSQHE NKDMLRFITC GSVDDGKSTL IGRLLHDSKL IFEDQLAAIE 

        70         80         90        100        110        120 
RDSKKYNTTD QDIDLALLVD GLQAEREQGI TIDVAYRYFS TDKRKFIIAD CPGHEQYTRN 

       130        140        150        160        170        180 
MATGASTSNL AIILIDARRG VQTQTRRHSY IVSLLGIRHV IVAVNKMDLV DYSEDVYNRI 

       190        200        210        220        230        240 
RDEYLTFAEH LDIPDIHFVP ISALRGDNVV SRTEAAPWYQ GATLMHLLET VQISHDAPLS 

       250        260        270        280        290        300 
AFRLPVQYVN RPNLDFRGFC GTIASGAVHP GDAVVALPSG KESRVKEIVT FDGSLSRAGA 

       310        320        330        340        350        360 
GQAVTLTLED EIDISRGDML VRADEARPHV SRSFDAHLVA MGEAPLRPGK EYGFKLAGKY 

       370        380        390        400        410        420 
VTGRIEAILH RTDVNTLQDS PADALALNEI GLCRISLNSP AAFDAYRDCR GSGSLILIDR 

       430        440        450        460        470 
LSNGTVAAGM IVAQSEEASP AALSPWALFE QELDQLLQRY FPQMTRAELA RRLRDEL 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ59979.1.
RefSeqNP_901977.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NVN5.
SMRQ7NVN5. Positions 16-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_2307.

Proteomic databases

PRIDEQ7NVN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ59979; AAQ59979; CV_2307.
GeneID2549880.
KEGGcvi:CV_2307.
PATRIC21439382. VBIChrVio67196_2247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2895.
HOGENOMHOG000229289.
KOK00956.
OMAWSESAFR.
OrthoDBEOG6GR38Q.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-2362-MONOMER.
UniPathwayUPA00140; UER00204.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00062. Sulf_adenylyltr_sub1.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR011779. SO4_adenylTrfase_lsu.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR02034. CysN. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSN_CHRVO
AccessionPrimary (citable) accession number: Q7NVN5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways