(data stored in SCRATCH3701 zone)

SWISSPROT: ARAB_ECOBW

ID   ARAB_ECOBW              Reviewed;         566 AA.
AC   C4ZPY6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 59.
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=BWG_0059;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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}.
DR   EMBL; CP001396; ACR63676.1; -; Genomic_DNA.
DR   RefSeq; WP_000951785.1; NC_012759.1.
DR   EnsemblBacteria; ACR63676; ACR63676; BWG_0059.
DR   KEGG; ebw:BWG_0059; -.
DR   HOGENOM; HOG000236883; -.
DR   KO; K00853; -.
DR   OMA; FTACTML; -.
DR   BioCyc; ECOL595496:BWG_RS00320-MONOMER; -.
DR   UniPathway; UPA00145; UER00566.
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; C4ZPY6.
DR   SWISS-2DPAGE; C4ZPY6.
KW   Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..566
FT                   /note="Ribulokinase"
FT                   /id="PRO_1000211744"
SQ   SEQUENCE   566 AA;  61157 MW;  4BAD2C547565E77A CRC64;
     MAIAIGLDFG SDSVRALAVD CASGEEIATS VEWYPRWQKG QFCDAPNNQF RHHPRDYIES
     MEAALKTVLA ELSVEQRAAV VGIGVDSTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
     DHTAVERSEE ITRLCHAPGN VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQSAASWIEL
     CDWVPALLSG TTRPQDIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPIL NRHLPSPLFT
     DTWTADIPVG TLCPEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNALV KVIGTSTCDI
     LIADKQSVGE RAVKGICGQV DGSVVPGFIG LEAGQSAFGD IYAWFGRVLS WPLEQLAAQH
     PELKAQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRSPNANQRL KGVITDLNLA
     TDAPLLFGGL IAATAFGARA IMECFTDQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPRSEQAQ RFEQLYRRYQ
     QWAMSAEQHY LPTSAPAQAA QAVATL
//

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