YAGF_ECOLI
ID YAGF_ECOLI Reviewed; 655 AA.
AC P77596; Q2MCF3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=D-xylonate dehydratase YagF {ECO:0000305};
DE EC=4.2.1.82 {ECO:0000305|PubMed:23233208};
GN Name=yagF; OrderedLocusNames=b0269, JW0262;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=23233208; DOI=10.1007/s00253-012-4618-7;
RA Liu H., Ramos K.R., Valdehuesa K.N., Nisola G.M., Lee W.K., Chung W.J.;
RT "Biosynthesis of ethylene glycol in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 97:3409-3417(2013).
RN [5]
RP INDUCTION.
RX PubMed=29087459; DOI=10.1093/femsle/fnx220;
RA Shimada T., Momiyama E., Yamanaka Y., Watanabe H., Yamamoto K.,
RA Ishihama A.;
RT "Regulatory role of XynR (YagI) in catabolism of xylonate in Escherichia
RT coli K-12.";
RL FEMS Microbiol. Lett. 364:0-0(2017).
CC -!- FUNCTION: Catalyzes the dehydration of D-xylonic acid to form 2-
CC dehydro-3-deoxy-D-pentonate. {ECO:0000305|PubMed:23233208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O;
CC Xref=Rhea:RHEA:19157, ChEBI:CHEBI:15377, ChEBI:CHEBI:16699,
CC ChEBI:CHEBI:17746; EC=4.2.1.82;
CC Evidence={ECO:0000305|PubMed:23233208};
CC -!- INDUCTION: Expression is repressed by the transcriptional regulator
CC XynR. {ECO:0000269|PubMed:29087459}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant has reduced ability to
CC catabolize D-xylonic acid. YjhG-yagF double mutant cannot use D-
CC xylonate as the sole source of carbon. {ECO:0000269|PubMed:23233208}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000305}.
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DR EMBL; U70214; AAB08690.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73372.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76053.1; -; Genomic_DNA.
DR PIR; E64752; E64752.
DR RefSeq; NP_414803.1; NC_000913.3.
DR RefSeq; WP_000151261.1; NZ_LN832404.1.
DR AlphaFoldDB; P77596; -.
DR SMR; P77596; -.
DR BioGRID; 4261825; 9.
DR STRING; 511145.b0269; -.
DR PaxDb; P77596; -.
DR PRIDE; P77596; -.
DR EnsemblBacteria; AAC73372; AAC73372; b0269.
DR EnsemblBacteria; BAE76053; BAE76053; BAE76053.
DR GeneID; 944928; -.
DR KEGG; ecj:JW0262; -.
DR KEGG; eco:b0269; -.
DR PATRIC; fig|511145.12.peg.273; -.
DR EchoBASE; EB3129; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_5_0_6; -.
DR OMA; MEHFHHA; -.
DR PhylomeDB; P77596; -.
DR BioCyc; EcoCyc:G6141-MON; -.
DR BioCyc; MetaCyc:G6141-MON; -.
DR PRO; PR:P77596; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0050401; F:xylonate dehydratase activity; IDA:EcoCyc.
DR GO; GO:0046176; P:aldonic acid catabolic process; IMP:EcoCyc.
DR Gene3D; 3.50.30.80; -; 1.
DR InterPro; IPR017798; Dehydratase_YjhG/YagF.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR TIGRFAMs; TIGR03432; yjhG_yagF; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..655
FT /note="D-xylonate dehydratase YagF"
FT /id="PRO_0000103560"
SQ SEQUENCE 655 AA; 69399 MW; 208AF2F6DB39EE8B CRC64;
MTIEKIFTPQ DDAFYAVITH AAGPQGALPL TPQMLMESPS GNLFGMTQNA GMGWDANKLT
GKEVLIIGTQ GGIRAGDGRP IALGYHTGHW EIGMQMQAAA KEITRNGGIP FAAFVSDPCD
GRSQGTHGMF DSLPYRNDAA IVFRRLIRSL PTRRAVIGVA TCDKGLPATM IALAAMHDLP
TILVPGGATL PPTVGEDAGK VQTIGARFAN HELSLQEAAE LGCRACASPG GGCQFLGTAG
TSQVVAEALG LALPHSALAP SGQAVWLEIA RQSARAVSEL DSRGITTRDI LSDKAIENAM
VIHAAFGGST NLLLHIPAIA HAAGCTIPDV EHWTRINRKV PRLVSVLPNG PDYHPTVRAF
LAGGVPEVML HLRDLGLLHL DAMTVTGQTV GENLEWWQAS ERRARFRQCL REQDGVEPDD
VILPPEKAKA KGLTSTVCFP TGNIAPEGSV IKATAIDPSV VGEDGVYHHT GRVRVFVSEA
QAIKAIKREE IVQGDIMVVI GGGPSGTGME ETYQLTSALK HISWGKTVSL ITDARFSGVS
TGACFGHVSP EALAGGPIGK LRDNDIIEIA VDRLTLTGSV NFIGTADNPL TPEEGARELA
RRQTHPDLHA HDFLPDDTRL WAALQSVSGG TWKGCIYDTD KIIEVINAGK KALGI
