ID   ARAB_SALA4              Reviewed;         569 AA.
AC   B5F784;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=SeAg_B0114;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH49543.1; -; Genomic_DNA.
DR   RefSeq; WP_000951827.1; NC_011149.1.
DR   AlphaFoldDB; B5F784; -.
DR   SMR; B5F784; -.
DR   EnsemblBacteria; ACH49543; ACH49543; SeAg_B0114.
DR   KEGG; sea:SeAg_B0114; -.
DR   HOGENOM; CLU_009281_9_1_6; -.
DR   OMA; GHKAMWH; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000008819; 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..569
FT                   /note="Ribulokinase"
FT                   /id="PRO_1000127636"
SQ   SEQUENCE   569 AA;  61729 MW;  604EF23CF0CF8086 CRC64;
     MAIAIGLDFG SDSVRALAVD CATGDEIATS VEWYPRWQEG RYCDGPNNQF RHHPRDYMES
     MEAALKAVLA QLSSAQRANV VGIGVDSTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
     DHTAVEEADE ITRLCHKPGK VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQAAVSWIEL
     CDWVPALLSG TTRPQDIRRG RCSAGHKTLW HESWGGLPPS SFFDELDPCI NRHLRYPLFS
     ETFTADLPVG TLCAEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNTLV KVIGTSTCDI
     LIADKQSVGD RAVKGICGQV DGSVVPNFIG LEAGQSAFGD IYAWFSRVLS WPLEQLAAQH
     PELKTQINAS QKQLLPALTD AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
     TDAPALFGGL VASTAFGARA IQECFTDQGI AVNNVMALGG IARKNQVIMQ VCCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AKIHADIPAA QQSMASAVER TLRPRPEQAQ RLEQLYRRYQ
     QWALSAEQHY LPTAAPAPTT PANQAILTH