ID   ARAB_STAAW              Reviewed;         545 AA.
AC   Q8NXY1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=MW0507;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB94372.1; -; Genomic_DNA.
DR   RefSeq; WP_000122337.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXY1; -.
DR   SMR; Q8NXY1; -.
DR   EnsemblBacteria; BAB94372; BAB94372; BAB94372.
DR   KEGG; sam:MW0507; -.
DR   HOGENOM; CLU_009281_9_1_9; -.
DR   OMA; GHKAMWH; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000000418; 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_0000198371"
SQ   SEQUENCE   545 AA;  60967 MW;  9DFD11D67B668C74 CRC64;
     MSYSIGIDYG TASGRVFLIN TTNGQVVSKF VKPYTHGVIE SELNGLKIPH TYALQNSNDY
     LEIMEEGISY IVRESKIDPD NIVGIGIDFT SSTIIFTDEN LNPVHNLKQF KNNPHAYVKL
     WKHHGAYKEA EKLYQTAIEN NNKWLGHYGY NVSSEWMIPK IMEVMNRAPE IMEKTAYIME
     AGDWIVNKLT NKNIRSNCGL GFKAFWEEET GFHYDLFDKI DPKLSKVIQD KVSAPVVNIG
     EAVGKLDDKM AQKLGLSKET MVSPFIIDAH ASLLGIGSEK DKEMTMVMGT STCHLMLNEK
     QHQVPGISGS VKGAIIPELF AYEAGQSAVG DLFEYVAKQA PKSYVDEAAN RNMTVFELMN
     EKIKHQMPGE SGLIALDWHN GNRSVLSDSN LTGCIFGLTL QTKHEDIYRA YLEATAFGTK
     MIMQQYQDWH MEVEKVFACG GIPKKNAVMM DIYANVLNKK LIVMDSEYAP AIGAAILGAV
     SGGAHNSIND AVDAMKEPIL YEINPEAEKV QRYETLFKAY KALHDIHGYK KANIMKDIQS
     LRVEG