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UniProtKB/Swiss-Prot entry Q10600

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYSNC_MYCTU
Primary accession number Q10600
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 69)
Name and origin of the protein
Protein name Bifunctional enzyme cysN/cysC
Synonyms None
Includes Sulfate adenylyltransferase subunit 1
     (EC 2.7.7.4)
     (Sulfate adenylate transferase)
     (SAT)
     (ATP-sulfurylase large subunit)
Adenylyl-sulfate kinase
     (EC 2.7.1.25)
     (APS kinase)
     (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase)
Gene name
Name: cysNC
Synonyms: cysN
OrderedLocusNames: Rv1286, MT1324
ORFNames: MTCY373.05
From
Mycobacterium tuberculosis [TaxID: 1773] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.";
Nature 393:537-544(1998).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
Comments
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
BX842576; CAA97752.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK45585.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B70772; B70772.
RefSeq NP_215802.1; -.
NP_335771.1; -.
3D structure databases
HSSP Q12657; 1M7G. [HSSP ENTRY / PDB]
ModBase Q10600.
Organism-specific databases
TubercuList Rv1286; -.
Ontologies
GO
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:0005525; Molecular function: GTP binding (inferred from electronic annotation from HAMAP).
GO:0003924; Molecular function: GTPase activity (inferred from electronic annotation from InterPro).
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).
QuickGo view.
Family and domain databases
HAMAP MF_00062; fused; 1.
MF_00065; fused; 1.
PBIL [Tree]
InterPro IPR002891; APS_kinase_C.
IPR011779; CysNAde_trans.
IPR000795; ProtSyn_GTP_bd.
IPR004161; Transl_elong_EFTu/EF1A_2.
Graphical view of domain structure.
Pfam PF01583; APS_kinase; 1.
PF00009; GTP_EFTU; 1.
PF03144; GTP_EFTU_D2; 1.
Pfam graphical view of domain structure.
PRINTS PR00315; ELONGATNFCT.
ProDom PD002350; APS_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00455; apsK; 1.
TIGR02034; CysN; 1.
PROSITE PS00301; EFACTOR_GTP; 1.
ProtoNet Q10600.
Genome annotation databases
GeneID 886978; -.
924747; -.
GenomeReviews AE000516_GR; MT1324.
AL123456_GR; Rv1286.
KEGG mtc:MT1324; -.
mtu:Rv1286; -.
TIGR MT1324; -.
Phylogenomic databases
HOGENOM Q10600; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; GTP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   614  614     Bifunctional enzyme cysN/cysC. PRO_0000091537
NP_BIND   11    18  8     GTP (By similarity). 
NP_BIND   88    92  5     GTP (By similarity). 
NP_BIND   143   146  4     GTP (By similarity). 
NP_BIND   450   457  8     ATP (Potential). 
REGION   1   441  441     Sulfate adenylyltransferase. 
REGION   442   614  173     Adenylyl-sulfate kinase. 
ACT_SITE   524   524        Phosphoserine intermediate (By similarity). 
Sequence information
Length: 614 AA [This is the length of the unprocessed precursor] Molecular weight: 67839 Da [This is the MW of the unprocessed precursor] CRC64: 2C3709C8B91867C4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTTLLRLATA GSVDDGKSTL IGRLLYDSKA VMEDQWASVE QTSKDRGHDY TDLALVTDGL 

        70         80         90        100        110        120 
RAEREQGITI DVAYRYFATP KRKFIIADTP GHIQYTRNMV TGASTAQLVI VLVDARHGLL 

       130        140        150        160        170        180 
EQSRRHAFLA SLLGIRHLVL AVNKMDLLGW DQEKFDAIRD EFHAFAARLD VQDVTSIPIS 

       190        200        210        220        230        240 
ALHGDNVVTK SDQTPWYEGP SLLSHLEDVY IAGDRNMVDV RFPVQYVIRP HTLEHQDHRS 

       250        260        270        280        290        300 
YAGTVASGVM RSGDEVVVLP IGKTTRITAI DGPNGPVAEA FPPMAVSVRL ADDIDISRGD 

       310        320        330        340        350        360 
MIARTHNQPR ITQEFDATVC WMADNAVLEP GRDYVVKHTT RTVRARIAGL DYRLDVNTLH 

       370        380        390        400        410        420 
RDKTATALKL NELGRVSLRT QVPLLLDEYT RNASTGSFIL IDPDTNGTVA AGMVLRDVSA 

       430        440        450        460        470        480 
RTPSPNTVRH RSLVTAQDRP PRGKTVWFTG LSGSGKSSVA MLVERKLLEK GISAYVLDGD 

       490        500        510        520        530        540 
NLRHGLNADL GFSMADRAEN LRRLSHVATL LADCGHLVLV PAISPLAEHR ALARKVHADA 

       550        560        570        580        590        600 
GIDFFEVFCD TPLQDCERRD PKGLYAKARA GEITHFTGID SPYQRPKNPD LRLTPDRSID 

       610 
EQAQEVIDLL ESSS
Q10600 in FASTA format

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