ARAB_ECO45
ID ARAB_ECO45 Reviewed; 566 AA.
AC B7MAI6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, 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=ECS88_0066;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR01432.1; -; Genomic_DNA.
DR RefSeq; WP_000951841.1; NC_011742.1.
DR AlphaFoldDB; B7MAI6; -.
DR SMR; B7MAI6; -.
DR EnsemblBacteria; CAR01432; CAR01432; ECS88_0066.
DR KEGG; ecz:ECS88_0066; -.
DR HOGENOM; CLU_009281_9_1_6; -.
DR OMA; GHKAMWH; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000000747; 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..566
FT /note="Ribulokinase"
FT /id="PRO_1000127626"
SQ SEQUENCE 566 AA; 61196 MW; D4F27FDB6D60FB77 CRC64;
MAIAIGLDFG SDSVRALAVD CATGEEIATS VEWYPRWQKG QFCDAPNNQF RHHPRDYIES
MEAALKTVLA ELSAEQRAAV VGIGVDTTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
DHTAVEEAEE ITRLCHAPGN VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQSAASWIEL
CDWVPALLSG TTRPQDIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPIL NRHLPSPLFT
DTWTADIPVG TLCPEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNALV KVIGTSTCDI
LIADKQSVGE RAVKGICGQV DGSVVPGFIG LEAGQSAFGD IYAWFGRVLS WPLEQLAAQH
PELKEQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
TDAPLLFGGL IAATAFGARA IMECFTDQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL
QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPRSEQAQ RFEQLYRRYQ
QWAMSAEQHY PPTSAPAQAA QAVPTL