(data stored in ACNUC7421 zone)

SWISSPROT: ARAB_ECO27

ID   ARAB_ECO27              Reviewed;         566 AA.
AC   B7UIA9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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=E2348C_0064;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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
CC       route): step 2/3. {ECO:0000255|HAMAP-Rule:MF_00520}.
CC   -!- SIMILARITY: Belongs to the ribulokinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00520}.
DR   EMBL; FM180568; CAS07612.1; -; Genomic_DNA.
DR   RefSeq; WP_000951866.1; NC_011601.1.
DR   EnsemblBacteria; CAS07612; CAS07612; E2348C_0064.
DR   KEGG; ecg:E2348C_0064; -.
DR   KO; K00853; -.
DR   OMA; IILWMDH; -.
DR   BioCyc; ECOL574521:E2348C_RS00330-MONOMER; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR005929; Ribulokinase.
DR   Pfam; PF02782; FGGY_C; 1.
DR   TIGRFAMs; TIGR01234; L-ribulokinase; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIA9.
DR   SWISS-2DPAGE; B7UIA9.
KW   Arabinose catabolism; ATP-binding; Carbohydrate metabolism;
KW   Complete proteome; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    566       Ribulokinase.
FT                                /FTId=PRO_1000189553.
SQ   SEQUENCE   566 AA;  61237 MW;  1FCD2D3C44959002 CRC64;
     MAIAIGLDFG SDSVRALAVD CATGEEIATS VEWYPRWQNG QFCDAPNNQF RHHPRDYIES
     MEAALKTVLA ELSVEQRAAV VGIGVDTTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
     DHTAVEEAEE ITRLCHTPGN VDYSRYIGGI YSSEWFWAKI LHVTRQDNAV AQSAASWIEL
     CDWVPALLSG TTRPQDIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPIL NRHLPSPLFT
     ETWTADIPVG TLCPEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNALV KVIGTSTCDI
     LIADKQSVGE RAVKGICGQV DGSVVPGFIG LEAGQSAFGD IYAWFGRVLG WPLEQLAAQH
     PELKEQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
     TDAPLLFGGL IAATAFGARA IMECFTAQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPRSEQAQ RFEPLYRRYQ
     QWAMSAEQHY LPTSAPAQAD QAVPTL
//

If you have problems or comments...

PBIL Back to PBIL home page