YJHH_ECOLI
ID YJHH_ECOLI Reviewed; 301 AA.
AC P39359; Q2M617;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable 2-dehydro-3-deoxy-D-pentonate aldolase YjhH {ECO:0000305};
DE EC=4.1.2.28 {ECO:0000305|PubMed:23233208};
GN Name=yjhH; OrderedLocusNames=b4298, JW5775;
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].
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).
CC -!- FUNCTION: Functions as a 2-dehydro-3-deoxy-D-pentonate aldolase.
CC {ECO:0000305|PubMed:23233208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-arabinonate = glycolaldehyde + pyruvate;
CC Xref=Rhea:RHEA:20609, ChEBI:CHEBI:15361, ChEBI:CHEBI:16699,
CC ChEBI:CHEBI:17071; EC=4.1.2.28;
CC Evidence={ECO:0000305|PubMed:23233208};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant has reduced ability to
CC catabolize D-xylonic acid. YjhH-yagE double mutant cannot use D-
CC xylonate as the sole source of carbon. {ECO:0000269|PubMed:23233208}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97194.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97194.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77254.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78289.1; -; Genomic_DNA.
DR PIR; S56523; S56523.
DR RefSeq; NP_418718.4; NC_000913.3.
DR RefSeq; WP_000714563.1; NZ_SSUV01000012.1.
DR AlphaFoldDB; P39359; -.
DR SMR; P39359; -.
DR BioGRID; 4260972; 5.
DR DIP; DIP-12622N; -.
DR IntAct; P39359; 1.
DR STRING; 511145.b4298; -.
DR PaxDb; P39359; -.
DR PRIDE; P39359; -.
DR EnsemblBacteria; AAC77254; AAC77254; b4298.
DR EnsemblBacteria; BAE78289; BAE78289; BAE78289.
DR GeneID; 948825; -.
DR KEGG; ecj:JW5775; -.
DR KEGG; eco:b4298; -.
DR PATRIC; fig|511145.12.peg.4434; -.
DR EchoBASE; EB2438; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_6; -.
DR InParanoid; P39359; -.
DR OMA; WCTAAPC; -.
DR PhylomeDB; P39359; -.
DR BioCyc; EcoCyc:G7911-MON; -.
DR BioCyc; MetaCyc:G7911-MON; -.
DR PRO; PR:P39359; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047440; F:2-dehydro-3-deoxy-D-pentonate aldolase activity; IMP:EcoCyc.
DR GO; GO:0046176; P:aldonic acid catabolic process; IMP:EcoCyc.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR PROSITE; PS00665; DHDPS_1; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..301
FT /note="Probable 2-dehydro-3-deoxy-D-pentonate aldolase
FT YjhH"
FT /id="PRO_0000103245"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P75682"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P75682"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P75682"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250|UniProtKB:P75682"
SQ SEQUENCE 301 AA; 32722 MW; A83BE11A0B134E46 CRC64;
MKKFSGIIPP VSSTFHRDGT LDKKAMREVA DFLINKGVDG LFYLGTGGEF SQMNTAQRMA
LAEEAVTIVD GRVPVLIGVG SPSTDEAVKL AQHAQAYGAD GIVAINPYYW KVAPRNLDDY
YQQIARSVTL PVILYNFPDL TGQDLTPETV TRLALQNENI VGIKDTIDSV GHLRTMINTV
KSVRPSFSVF CGYDDHLLNT MLLGGDGAIT ASANFAPELS VGIYRAWREG DLATAATLNK
KLLQLPAIYA LETPFVSLIK YSMQCVGLPV ETYCLPPILE ASEEAKDKVH VLLTAQGILP
V
