ID   ARAB_YERPA              Reviewed;         567 AA.
AC   Q1C7J2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=YPA_1614;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG13580.1; -; Genomic_DNA.
DR   RefSeq; WP_002210590.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C7J2; -.
DR   SMR; Q1C7J2; -.
DR   EnsemblBacteria; ABG13580; ABG13580; YPA_1614.
DR   GeneID; 57976416; -.
DR   KEGG; ypa:YPA_1614; -.
DR   OMA; GHKAMWH; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000001971; 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..567
FT                   /note="Ribulokinase"
FT                   /id="PRO_0000263410"
SQ   SEQUENCE   567 AA;  62205 MW;  A614A0434E334B5D CRC64;
     MTGNVISADG AIALGLDFGS DSVRVLAVDC QHGTEIDTEV VYYPRWKKGL YCQAAQNQFR
     HHPLDYIEAM EQAIRQMVKR LSEEQRQHIV GIGVDSTGST PAPIDEQGQV LALRPDFADN
     PNAMFVLWKD HTAIEEAEEI NRLCRSGEFA DYSRYIGGVY SSEWFWAKIL HVTRADVAVR
     EAAVSWIELC DWVPALLSGT TAPQDIQRGR CSAGHKSLWH PSWGGLPPRA FLAALDTSLV
     NDLDYPMFTD TYTAERPVGQ ITAEWAERLG LPTTVILSGG AFDCHMGAVG AGAQPYTLVK
     VIGTSTCDIL IADDQRVGDR AIAGICGQVE GSVLPGWIGM EAGQSAFGDM YAWFSNLLSW
     PLHQAALTQP EWQPQLKQIE SNLLASLTRA WAQNPSLDHL PVVLDWFNGR RTPNANQRLK
     GVITDLNLGT DAPTLFGGFI AATAFGARAI MECFEQQDIP IDNVLALGGI ARKSPVIMQV
     CADVMNRPLQ IVASDQCCAL GAAIFAAVAA GAHDDVPTAQ RHMACNIERT LIPDPVQVVR
     YQQLYQRYQQ WCHTAEPHYA PVTKVIH