ID   ARAB_SALPA              Reviewed;         569 AA.
AC   Q5PDF1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   02-SEP-2026, entry version 98.
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};
GN   OrderedLocusNames=SPA0105;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose + ATP = D-ribulose 5-phosphate + ADP + 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=L-ribulose + ATP = L-ribulose 5-phosphate + ADP + H(+);
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; CP000026; AAV76138.1; -; Genomic_DNA.
DR   RefSeq; WP_000951819.1; NC_006511.1.
DR   AlphaFoldDB; Q5PDF1; -.
DR   SMR; Q5PDF1; -.
DR   KEGG; spt:SPA0105; -.
DR   HOGENOM; CLU_009281_9_1_6; -.
DR   UniPathway; UPA00145; UER00566.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0019150; F:D-ribulokinase activity; IEA:TreeGrafter.
DR   GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IEA:TreeGrafter.
DR   GO; GO:0019569; P:L-arabinose catabolic process to D-xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR   CDD; cd07781; ASKHA_NBD_FGGY_L-RBK; 1.
DR   Gene3D; 1.20.58.2240; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   HAMAP; MF_00520; Ribulokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR005929; Ribulokinase.
DR   NCBIfam; TIGR01234; L-ribulokinase; 1.
DR   NCBIfam; NF003154; PRK04123.1; 1.
DR   PANTHER; PTHR43435:SF4; FGGY CARBOHYDRATE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43435; RIBULOKINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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_0000263403"
SQ   SEQUENCE   569 AA;  61759 MW;  25913906ADA2A42E 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 IQECFTEQGI AVNNVMALGG IARKNQVIMQ VCCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AKVHADIPAA QQSMASAVER TLRPRPEQAQ RFERLYRRYQ
     QWALSAEQHY LPTAAPAPTT PANQAILTH
//