ID   ARAB_SALSV              Reviewed;         569 AA.
AC   B4TWU9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=SeSA_A0114;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
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; CP001127; ACF91969.1; -; Genomic_DNA.
DR   RefSeq; WP_000951817.1; NC_011094.1.
DR   AlphaFoldDB; B4TWU9; -.
DR   SMR; B4TWU9; -.
DR   EnsemblBacteria; ACF91969; ACF91969; SeSA_A0114.
DR   KEGG; sew:SeSA_A0114; -.
DR   HOGENOM; CLU_009281_9_1_6; -.
DR   OMA; GHKAMWH; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000001865; 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_1000127643"
SQ   SEQUENCE   569 AA;  61683 MW;  A62139B451837ACE CRC64;
     MAIAIGLDFG SDSVRALAVD CATGDEIATS VEWYPRWQEG RYCDGPNNQF RHHPRDYMES
     MEAALKAVLA QLSAAQRANV VGIGVDSTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
     DHTAVEEADE ITRLCHKPGK VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQAAVSWIEL
     CDWVPALLSG TTRPQDIRRG RCSAGHKTLW HESWGGLPPA 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 AKVHADIPAA QQSMASAVER TLRPRPEQAQ RLEQLYRRYQ
     QWALSAEQHY LPTAAPAPTT PANQAILTH