ARAB_ECOLI
ID ARAB_ECOLI Reviewed; 566 AA.
AC P08204; P78041;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ribulokinase;
DE EC=2.7.1.16;
GN Name=araB; OrderedLocusNames=b0063, JW0062;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3549454; DOI=10.1016/0378-1119(86)90067-3;
RA Lee N., Gielow W., Martin R., Hamilton E., Fowler A.;
RT "The organization of the araBAD operon of Escherichia coli.";
RL Gene 47:231-244(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-14, AND PROTEIN SEQUENCE OF 2-14.
RX PubMed=189315; DOI=10.1073/pnas.74.1.49;
RA Lee N., Carbon J.;
RT "Nucleotide sequence of the 5' end of araBAD operon messenger RNA in
RT Escherichia coli B/r.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:49-53(1977).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC STRAIN=K12;
RX PubMed=357433; DOI=10.1016/s0021-9258(17)38009-2;
RA Smith B.R., Schleif R.;
RT "Nucleotide sequence of the L-arabinose regulatory region of Escherichia
RT coli K12.";
RL J. Biol. Chem. 253:6931-6933(1978).
RN [7]
RP INDUCTION.
RX PubMed=328165; DOI=10.1016/0092-8674(77)90072-1;
RA Hirsh J., Schleif R.;
RT "The araC promoter: transcription, mapping and interaction with the araBAD
RT promoter.";
RL Cell 11:545-550(1977).
RN [8]
RP INDUCTION.
RX PubMed=2962192; DOI=10.1073/pnas.84.24.8814;
RA Lee N., Francklyn C., Hamilton E.P.;
RT "Arabinose-induced binding of AraC protein to araI2 activates the araBAD
RT operon promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8814-8818(1987).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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;
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;
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 2/3.
CC -!- INDUCTION: Induced by arabinose. Transcription is dependent on the
CC transcription factor AraC, the cAMP receptor protein (CRP) and cAMP.
CC {ECO:0000269|PubMed:2962192, ECO:0000269|PubMed:328165}.
CC -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000305}.
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DR EMBL; M15263; AAA23462.1; -; Genomic_DNA.
DR EMBL; J01641; AAA23467.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73174.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96632.2; -; Genomic_DNA.
DR EMBL; K01304; AAA23465.1; -; mRNA.
DR PIR; G64727; KIECRU.
DR RefSeq; NP_414605.1; NC_000913.3.
DR RefSeq; WP_000951856.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P08204; -.
DR SMR; P08204; -.
DR IntAct; P08204; 1.
DR STRING; 511145.b0063; -.
DR PaxDb; P08204; -.
DR PRIDE; P08204; -.
DR DNASU; 946017; -.
DR EnsemblBacteria; AAC73174; AAC73174; b0063.
DR EnsemblBacteria; BAB96632; BAB96632; BAB96632.
DR GeneID; 946017; -.
DR KEGG; ecj:JW0062; -.
DR KEGG; eco:b0063; -.
DR PATRIC; fig|1411691.4.peg.2220; -.
DR EchoBASE; EB0051; -.
DR eggNOG; COG1069; Bacteria.
DR HOGENOM; CLU_009281_9_1_6; -.
DR InParanoid; P08204; -.
DR OMA; GHKAMWH; -.
DR PhylomeDB; P08204; -.
DR BioCyc; EcoCyc:RIBULOKIN-MON; -.
DR BioCyc; MetaCyc:RIBULOKIN-MON; -.
DR UniPathway; UPA00145; UER00566.
DR PRO; PR:P08204; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019150; F:D-ribulokinase activity; IBA:GO_Central.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:EcoliWiki.
DR GO; GO:0008741; F:ribulokinase activity; IDA:EcoCyc.
DR GO; GO:0019568; P:arabinose catabolic process; IDA:EcoliWiki.
DR GO; GO:0016052; P:carbohydrate catabolic process; IDA:EcoliWiki.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0019572; P:L-arabinose catabolic process; IDA:EcoliWiki.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEP:EcoCyc.
DR GO; GO:0019321; P:pentose metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Arabinose catabolism; ATP-binding; Carbohydrate metabolism;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:189315"
FT CHAIN 2..566
FT /note="Ribulokinase"
FT /id="PRO_0000198358"
FT CONFLICT 23
FT /note="T -> S (in Ref. 1; AAA23462)"
FT /evidence="ECO:0000305"
FT CONFLICT 127..128
FT /note="EA -> RS (in Ref. 1; AAA23462)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="G -> S (in Ref. 1; AAA23462)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="T -> A (in Ref. 1; AAA23462)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="T -> S (in Ref. 1; AAA23462)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="C -> R (in Ref. 1; AAA23462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 61089 MW; 4A12010092139D8A CRC64;
MAIAIGLDFG SDSVRALAVD CATGEEIATS VEWYPRWQKG QFCDAPNNQF RHHPRDYIES
MEAALKTVLA ELSVEQRAAV VGIGVDSTGS 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 IYAWFGRVLG WPLEQLAAQH
PELKTQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
TDAPLLFGGL IAATAFGARA IMECFTDQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL
QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPCSEQAQ RFEQLYRRYQ
QWAMSAEQHY LPTSAPAQAA QAVATL
