ID ARAB_STAAR Reviewed; 545 AA. AC Q6GJB6; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Ribulokinase; DE EC=2.7.1.16; GN Name=araB; OrderedLocusNames=SAR0557; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- CATALYTIC ACTIVITY: ATP + L(or D)-ribulose = ADP + L(or D)- CC ribulose 5-phosphate. CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L- CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacteria CC route): step 2/3. CC -!- SIMILARITY: Belongs to the ribulokinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571856; CAG39578.1; -; Genomic_DNA. DR RefSeq; YP_040006.1; -. DR GeneID; 2861089; -. DR GenomeReviews; BX571856_GR; SAR0557. DR KEGG; sar:SAR0557; -. DR HOGENOM; Q6GJB6; -. DR OMA; Q6GJB6; NGRRTPD. DR BioCyc; SAUR282458:SAR0557-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008741; F:ribulokinase activity; IEA:HAMAP. DR GO; GO:0019572; P:L-arabinose catabolic process; IEA:HAMAP. DR HAMAP; MF_00520; -; 1. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR PANTHER; PTHR10196; FGGY_kin; 1. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. PE 3: Inferred from homology; KW Arabinose catabolism; ATP-binding; Carbohydrate metabolism; KW Complete proteome; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1 545 Ribulokinase. FT /FTId=PRO_0000198369. SQ SEQUENCE 545 AA; 60909 MW; D2414579DDBE89F0 CRC64; MSYSIGIDYG TASGRVFLIN TTNGQVVSKF VKPYTHGVIE GELNGLKIPH TYALQNSNDY LEIMEEGISY IVRESKIDPV NIVGIGIDFT SSTIIFTDEN LNPVHNLKQF KNNPHAYVKL WKHHGAYKEA EKLYQTAIEN NNKWLGHYGY NVSSEWMIPK IMEVMNRAPE IMEKTAYIME AGDWIVNKLT NKNVRSNCGL GFKAFWEEET GFHYDLFDKV DPKLSKVIQD KVSAPVVNIG EAVGKLDDKM AQKLGLSKDT MVSPFIIDAH ASLLGIGSEK DKEMTMVMGT STCHLMLNEK QHQVPGISGS VKGAIIPELF AYEAGQSAVG DLFEYVAKQA PKSYVDEAAN RNMTVFELMN EKIKHQMPGE SGLIALDWHN GNRSVLSDSN LTGCIFGLTL QTKHEDIYRA YLEATAFGTK MIMQQYQDWH MEVEKVFACG GIPKKNAVMM DIYTNVLNKK LIVMDSEYAP AIGAAILGAV SGGAHNSIND AVDAMKEPIL YEINPEAEKV QRYETLFKAY KALHDIHGYK KANIMKDIQS LRVEG //