ID   ARAB_STAA1              Reviewed;         545 AA.
AC   A7WYY2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=SAHV_0550;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF77433.1; -; Genomic_DNA.
DR   RefSeq; WP_000122354.1; NC_009782.1.
DR   AlphaFoldDB; A7WYY2; -.
DR   SMR; A7WYY2; -.
DR   KEGG; saw:SAHV_0550; -.
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_1000050914"
SQ   SEQUENCE   545 AA;  60965 MW;  E3917036237CEA4B CRC64;
     MSYSIGIDYG TASGRVFLIN TTNGQVVSKF VKPYTHGVIE SELNGLKIPH TYALQNSNDY
     LEIMEEGISY IVRESKIDPV NIVGIGIDFT SSTIIFTDEN LNPVHNLKQF KNNPHAYVKL
     WKHHGAYKEA EKLYQTAIEN NNKWLGHYGY NVSSEWMIPK IMEVMNRAPE IMEKTAYIME
     AGDWIVNKLT NKNVRSNCGL GFKAFWEEET GFHYDLFDKI DPKLSKVIQD KVSAPVVNIG
     EVVGKLDDKM 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