ID   ARAB_STAAB              Reviewed;         545 AA.
AC   Q2YSA9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=SAB0503;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80191.1; -; Genomic_DNA.
DR   RefSeq; WP_000122345.1; NC_007622.1.
DR   AlphaFoldDB; Q2YSA9; -.
DR   SMR; Q2YSA9; -.
DR   KEGG; sab:SAB0503; -.
DR   HOGENOM; CLU_009281_9_1_9; -.
DR   OMA; GHKAMWH; -.
DR   UniPathway; UPA00145; UER00566.
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_0000263407"
SQ   SEQUENCE   545 AA;  60919 MW;  63D175628999BA9D CRC64;
     MSYSIGIDYG TASGRVFLIN TTNGQVVSKF VKPYTHGVIE SELNGLKIPH TYALQNSNDY
     LEIMEEGISY IVRESKIDPV NIVGIGIDFT SSTIIFTDEN INPVHNLKQF KNNPHAYVKL
     WKHHGAYKEA EKLYQTAIEN NNKWLGHYGY NVSSEWMIPK IMEVMNRAPE IMEKTAYIME
     AGDWIVNKLT NKNVRSNCGL GFKAFWEEET GFHYDLFDKI DPKLSKVIQD KVSAPVVNIG
     EAVGKLDDKM AQKLGLSKET MVSPFIIDAH ASLLGIGSEK DKEMTMVLGT 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