FUCK_ECOLI
ID FUCK_ECOLI Reviewed; 472 AA.
AC P11553; Q2MA31;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=L-fuculokinase {ECO:0000255|HAMAP-Rule:MF_00986};
DE EC=2.7.1.51 {ECO:0000255|HAMAP-Rule:MF_00986};
DE AltName: Full=L-fuculose kinase {ECO:0000255|HAMAP-Rule:MF_00986};
GN Name=fucK {ECO:0000255|HAMAP-Rule:MF_00986};
GN OrderedLocusNames=b2803, JW2774;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2664711; DOI=10.1093/nar/17.12.4883;
RA Lu Z., Lin E.C.C.;
RT "The nucleotide sequence of Escherichia coli genes for L-fucose
RT dissimilation.";
RL Nucleic Acids Res. 17:4883-4884(1989).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP POSSIBLE START SITE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9740056; DOI=10.1002/elps.1150191114;
RA Tonella L., Walsh B.J., Sanchez J.-C., Ou K., Wilkins M.R., Tyler M.,
RA Frutiger S., Gooley A.A., Pescaru I., Appel R.D., Yan J.X., Bairoch A.,
RA Hoogland C., Morch F.S., Hughes G.J., Williams K.L., Hochstrasser D.F.;
RT "'98 Escherichia coli SWISS-2DPAGE database update.";
RL Electrophoresis 19:1960-1971(1998).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PATHWAY.
RC STRAIN=O111:B4;
RX PubMed=13905785;
RA Heath E.C., Ghalambor M.A.;
RT "The metabolism of L-fucose. I. The purification and properties of L-
RT fuculose kinase.";
RL J. Biol. Chem. 237:2423-2426(1962).
RN [6]
RP POSSIBLE START SITE.
RX PubMed=25078267; DOI=10.1371/journal.pgen.1004463;
RA Schrader J.M., Zhou B., Li G.W., Lasker K., Childers W.S., Williams B.,
RA Long T., Crosson S., McAdams H.H., Weissman J.S., Shapiro L.;
RT "The coding and noncoding architecture of the Caulobacter crescentus
RT genome.";
RL PLoS Genet. 10:E1004463-E1004463(2014).
CC -!- FUNCTION: Catalyzes the phosphorylation of L-fuculose. Can also
CC phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-
CC fructose. {ECO:0000255|HAMAP-Rule:MF_00986,
CC ECO:0000269|PubMed:13905785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate;
CC Xref=Rhea:RHEA:12376, ChEBI:CHEBI:15378, ChEBI:CHEBI:17617,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57846, ChEBI:CHEBI:456216;
CC EC=2.7.1.51; Evidence={ECO:0000255|HAMAP-Rule:MF_00986,
CC ECO:0000269|PubMed:13905785};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00986,
CC ECO:0000269|PubMed:13905785};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:13905785};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC and glycerone phosphate from L-fucose: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_00986, ECO:0000269|PubMed:13905785}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00986}.
CC -!- CAUTION: A 10-residue longer version of this protein (starting with the
CC sequence MLSGYIAGAI) has been identified in strain W3110
CC (PubMed:9740056). Other evidence, including ribosomal profiling and
CC comparison with other bacterial genera, suggests this protein actually
CC starts on the indicated Met codon (PubMed:25078267).
CC {ECO:0000269|PubMed:25078267, ECO:0000269|PubMed:9740056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40453.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE76875.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA33128.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X15025; CAA33128.1; ALT_INIT; Genomic_DNA.
DR EMBL; U29581; AAB40453.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75845.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76875.1; ALT_INIT; Genomic_DNA.
DR PIR; JS0186; KIECFK.
DR RefSeq; NP_417283.2; NC_000913.3.
DR RefSeq; WP_000808392.1; NZ_LN832404.1.
DR AlphaFoldDB; P11553; -.
DR SMR; P11553; -.
DR BioGRID; 4259225; 22.
DR BioGRID; 850383; 1.
DR DIP; DIP-9712N; -.
DR IntAct; P11553; 4.
DR STRING; 511145.b2803; -.
DR SWISS-2DPAGE; P11553; -.
DR PaxDb; P11553; -.
DR PRIDE; P11553; -.
DR EnsemblBacteria; AAC75845; AAC75845; b2803.
DR EnsemblBacteria; BAE76875; BAE76875; BAE76875.
DR GeneID; 946022; -.
DR KEGG; ecj:JW2774; -.
DR KEGG; eco:b2803; -.
DR PATRIC; fig|511145.12.peg.2903; -.
DR EchoBASE; EB0346; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_11_2_6; -.
DR InParanoid; P11553; -.
DR PhylomeDB; P11553; -.
DR BioCyc; EcoCyc:FUCULOKIN-MON; -.
DR BioCyc; MetaCyc:FUCULOKIN-MON; -.
DR UniPathway; UPA00563; UER00625.
DR PRO; PR:P11553; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008737; F:L-fuculokinase activity; IDA:EcoCyc.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0019571; P:D-arabinose catabolic process; IMP:EcoCyc.
DR GO; GO:0042355; P:L-fucose catabolic process; IMP:EcoCyc.
DR GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central.
DR HAMAP; MF_00986; Fuculokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR013450; Fuculokinase.
DR PANTHER; PTHR10196:SF60; PTHR10196:SF60; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02628; fuculo_kin_coli; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Fucose metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..472
FT /note="L-fuculokinase"
FT /id="PRO_0000059423"
SQ SEQUENCE 472 AA; 52259 MW; E09BB640495D7A3D CRC64;
MKQEVILVLD CGATNVRAIA VNRQGKIVAR ASTPNASDIA MENNTWHQWS LDAILQRFAD
CCRQINSELT ECHIRGIAVT TFGVDGALVD KQGNLLYPII SWKCPRTAAV MDNIERLISA
QRLQAISGVG AFSFNTLYKL VWLKENHPQL LERAHAWLFI SSLINHRLTG EFTTDITMAG
TSQMLDIQQR DFSPQILQAT GIPRRLFPRL VEAGEQIGTL QNSAAAMLGL PVGIPVISAG
HDTQFALFGA GAEQNEPVLS SGTWEILMVR SAQVDTSLLS QYAGSTCELD SQAGLYNPGM
QWLASGVLEW VRKLFWTAET PWQMLIEEAR LIAPGADGVK MQCDLLSCQN AGWQGVTLNT
TRGHFYRAAL EGLTAQLQRN LQMLEKIGHF KASELLLVGG GSRNTLWNQI KANMLDIPVK
VLDDAETTVA GAALFGWYGV GEFNSPEEAR AQIHYQYRYF YPQTEPEFIE EV
