ID   ARAB_SALPB              Reviewed;         569 AA.
AC   A9MYN9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=SPAB_00130;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX65573.1; -; Genomic_DNA.
DR   RefSeq; WP_000951813.1; NC_010102.1.
DR   AlphaFoldDB; A9MYN9; -.
DR   SMR; A9MYN9; -.
DR   KEGG; spq:SPAB_00130; -.
DR   PATRIC; fig|1016998.12.peg.123; -.
DR   HOGENOM; CLU_009281_9_1_6; -.
DR   OMA; GHKAMWH; -.
DR   BioCyc; SENT1016998:SPAB_RS00510-MON; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000008556; 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_1000081682"
SQ   SEQUENCE   569 AA;  61746 MW;  F4DF06B55E04054B 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 DLPESVVISG GAFDCHMGAV GAGAQSNTLV KVIGTSTCDI
     LIADKQSVGD RAVKGICGQV DGSVVPNFIG LEAGQSAFGD IYAWFSRVLS WPLEQLAAQH
     PELKTQINAS QKQLLPALTD AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
     TDAPALFGGL VASTAFGARA IQECFTDQGI AVNNVMALGG IARKNQVIMQ VCCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AKVHADIPAA QQSMASAVER TLRPHPEQAQ RFEQLYRRYQ
     QWALSAEQHY LPTAAPAPTT PANQAILTH