ARAB_ECO24
ID ARAB_ECO24 Reviewed; 566 AA.
AC A7ZHF4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=EcE24377A_0065;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV20149.1; -; Genomic_DNA.
DR RefSeq; WP_000951798.1; NC_009801.1.
DR AlphaFoldDB; A7ZHF4; -.
DR SMR; A7ZHF4; -.
DR EnsemblBacteria; ABV20149; ABV20149; EcE24377A_0065.
DR KEGG; ecw:EcE24377A_0065; -.
DR HOGENOM; CLU_009281_9_1_6; -.
DR OMA; GHKAMWH; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000001122; 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_1000060917"
SQ SEQUENCE 566 AA; 61111 MW; E3EC05ABB06C7237 CRC64;
MAIAIGLDFG SDSVRALAVD CASGEEIATS VEWYPRWQKG QFCDAPNNQF RHHPRDYIES
MEAALKTVLA ELSVEQRAAV VGIGVDTTGS TPAPIDANGN VLALRPEFAE NPNAMFVLWK
DHTAVEEAEE ITRLCHAPGN VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQSAASWIEL
CDWVPALLSG TTRPQDIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPIL NRHLPSPLFT
DTWTADIPVG TLCPEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNALV KVIGTSTCDI
LIADKQSVGE RAVKGICGQV DGSVVPGFIG LEAGQSAFGD IYAWFGRVLG WPLEQLAAQH
PELKAQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
TDAPLLFGGL IAATAFGARA IMECFTDQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL
QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPRSEQAQ RFEQLYRRYQ
QWAMSAEQHY LPTSAPAQAA QAVATL