YJHG_ECOLI
ID YJHG_ECOLI Reviewed; 655 AA.
AC P39358; Q2M618;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=D-xylonate dehydratase YjhG {ECO:0000305|PubMed:26083940};
DE EC=4.2.1.82 {ECO:0000269|PubMed:26083940, ECO:0000305|PubMed:23233208};
GN Name=yjhG; OrderedLocusNames=b4297, JW4259;
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;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 555-556.
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=26083940; DOI=10.1080/21655979.2015.1040208;
RA Jiang Y., Liu W., Cheng T., Cao Y., Zhang R., Xian M.;
RT "Characterization of D-xylonate dehydratase YjhG from Escherichia coli.";
RL Bioengineered 6:227-232(2015).
CC -!- FUNCTION: Catalyzes the dehydration of D-xylonic acid to form 2-
CC dehydro-3-deoxy-D-pentonate. {ECO:0000269|PubMed:26083940,
CC 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:0000269|PubMed:26083940, ECO:0000305|PubMed:23233208};
CC -!- ACTIVITY REGULATION: Activity is increased in the presence of Mn(+) and
CC Mg(2+). Inhibited by thiol compounds. {ECO:0000269|PubMed:26083940}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.88 mM for D-xylonate {ECO:0000269|PubMed:26083940};
CC Note=kcat is 0.33 min(-1). {ECO:0000269|PubMed:26083940};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:26083940};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:26083940};
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; U14003; AAA97193.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77253.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78288.1; -; Genomic_DNA.
DR PIR; C65243; C65243.
DR RefSeq; NP_418717.1; NC_000913.3.
DR RefSeq; WP_000116326.1; NZ_SSUV01000012.1.
DR AlphaFoldDB; P39358; -.
DR SMR; P39358; -.
DR BioGRID; 4260973; 10.
DR BioGRID; 851170; 1.
DR IntAct; P39358; 4.
DR STRING; 511145.b4297; -.
DR jPOST; P39358; -.
DR PaxDb; P39358; -.
DR PRIDE; P39358; -.
DR EnsemblBacteria; AAC77253; AAC77253; b4297.
DR EnsemblBacteria; BAE78288; BAE78288; BAE78288.
DR GeneID; 946829; -.
DR KEGG; ecj:JW4259; -.
DR KEGG; eco:b4297; -.
DR PATRIC; fig|1411691.4.peg.2400; -.
DR EchoBASE; EB2437; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_5_0_6; -.
DR OMA; GSCMTMG; -.
DR PhylomeDB; P39358; -.
DR BioCyc; EcoCyc:G7910-MON; -.
DR BioCyc; MetaCyc:G7910-MON; -.
DR BRENDA; 4.2.1.82; 2026.
DR PRO; PR:P39358; -.
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 YjhG"
FT /id="PRO_0000103561"
FT CONFLICT 555..556
FT /note="GG -> EA (in Ref. 1; AAA97193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 70017 MW; 95F88200CB6EF14C CRC64;
MSVRNIFADE SHDIYTVRTH ADGPDGELPL TAEMLINRPS GDLFGMTMNA GMGWSPDELD
RDGILLLSTL GGLRGADGKP VALALHQGHY ELDIQMKAAA EVIKANHALP YAVYVSDPCD
GRTQGTTGMF DSLPYRNDAS MVMRRLIRSL PDAKAVIGVA SCDKGLPATM MALAAQHNIA
TVLVPGGATL PAKDGEDNGK VQTIGARFAN GELSLQDARR AGCKACASSG GGCQFLGTAG
TSQVVAEGLG LAIPHSALAP SGEPVWREIA RASARAALNL SQKGITTREI LTDKAIENAM
TVHAAFGGST NLLLHIPAIA HQAGCHIPTV DDWIRINKRV PRLVSVLPNG PVYHPTVNAF
MAGGVPEVML HLRSLGLLHE DVMTVTGSTL KENLDWWEHS ERRQRFKQLL LDQEQINADE
VIMSPQQAKA RGLTSTITFP VGNIAPEGSV IKSTAIDPSM IDEQGIYYHK GVAKVYLSEK
SAIYDIKHDK IKAGDILVII GVGPSGTGME ETYQVTSALK HLSYGKHVSL ITDARFSGVS
TGACIGHVGP EALAGGPIGK LRTGDLIEIK IDCRELHGEV NFLGTRSDEQ LPSQEEATAI
LNARPSHQDL LPDPELPDDT RLWAMLQAVS GGTWTGCIYD VNKIGAALRD FMNKN
