ARAB_STAAR
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 25-MAY-2022, entry version 84.
DE RecName: Full=Ribulokinase {ECO:0000255|HAMAP-Rule:MF_00520};
DE EC=2.7.1.16 {ECO:0000255|HAMAP-Rule:MF_00520};
GN Name=araB {ECO:0000255|HAMAP-Rule:MF_00520}; OrderedLocusNames=SAR0557;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-ribulose = ADP + H(+) + L-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:22072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16880,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58226, ChEBI:CHEBI:456216;
CC EC=2.7.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00520};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 2/3. {ECO:0000255|HAMAP-Rule:MF_00520}.
CC -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00520}.
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DR EMBL; BX571856; CAG39578.1; -; Genomic_DNA.
DR RefSeq; WP_000122332.1; NC_002952.2.
DR AlphaFoldDB; Q6GJB6; -.
DR SMR; Q6GJB6; -.
DR KEGG; sar:SAR0557; -.
DR HOGENOM; CLU_009281_9_1_9; -.
DR OMA; GHKAMWH; -.
DR OrthoDB; 1619686at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019150; F:D-ribulokinase activity; IEA:RHEA.
DR GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR CDD; cd07781; FGGY_RBK; 1.
DR HAMAP; MF_00520; Ribulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005929; Ribulokinase.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 3: Inferred from homology;
KW Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..545
FT /note="Ribulokinase"
FT /id="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