ID   ARAB_YERPS              Reviewed;         563 AA.
AC   Q66AF7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 85.
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=YPTB2173;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH21411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX936398; CAH21411.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q66AF7; -.
DR   SMR; Q66AF7; -.
DR   EnsemblBacteria; CAH21411; CAH21411; YPTB2173.
DR   KEGG; yps:YPTB2173; -.
DR   OMA; GHKAMWH; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000001011; 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; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR005929; Ribulokinase.
DR   Pfam; PF02782; FGGY_C; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01234; L-ribulokinase; 1.
PE   3: Inferred from homology;
KW   Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..563
FT                   /note="Ribulokinase"
FT                   /id="PRO_0000198378"
SQ   SEQUENCE   563 AA;  61766 MW;  B9FF9495BAD83DE4 CRC64;
     MISADGAIAL GLDFGSDSVR VLAVDCQHGT EIDTEVVYYP RWKKGLYCQA AQNQFRHHPL
     DYIEAMEQAI RQMVKRLSEE QRQHIVGIGV DSTGSTPAPI DEQGQVLALR PDFADNPNAM
     FVLWKDHTAI EEAEEINRLC RSGEFADYSR YIGGVYSSEW FWAKILHVTR ADVAVREAAV
     SWIELCDWVP ALLSGTTAPQ DIQRGRCSAG HKSLWHPSWG GLPPRAFLAA LDTSLVNDLD
     YPMFTDTYTA ERPVGQITAE WAERLGLPTT VILSGGAFDC HMGAVGAGAQ PYTLVKVIGT
     STCDILIADD QRVGDRAIAG ICGQVEGSVL PGWIGMEAGQ SAFGDMYAWF SNLLSWPLHQ
     AALTQPEWQP QLKQIESNLL ASLTCAWAQN PSLDHLPVVL DWFNGRRTPN ANQRLKGVIT
     DLNLGTDAPT LFGGFIAATA FGARAIMECF EQQDIPVENV LALGGIARKS PVIMQVCADV
     MNRPLQIVAS DQCCALGAAI FAAVAAGAHE DVPTAQRHMA CNIERTLIPD PVQVVRYQQL
     YQRYQQWCHT AEPHYAPVTK AIH