ID E3D9M9_GARV3 Unreviewed; 304 AA.
AC E3D9M9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Putative dihydrodipicolinate synthase {ECO:0000313|EMBL:ADP38773.1};
GN OrderedLocusNames=HMPREF0421_20691 {ECO:0000313|EMBL:ADP38773.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38773.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP38773.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP002104; ADP38773.1; -; Genomic_DNA.
DR RefSeq; WP_004117946.1; NC_014644.1.
DR RefSeq; YP_003985796.1; NC_014644.1.
DR AlphaFoldDB; E3D9M9; -.
DR KEGG; gvg:HMPREF0421_20691; -.
DR PATRIC; fig|525284.18.peg.685; -.
DR HOGENOM; CLU_049343_5_1_11; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000001453; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128:SF28; 2-DEHYDRO-3-DEOXY-D-GLUCONATE ALDOLASE YAGE-RELATED; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 174
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 219
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 304 AA; 32916 MW; 0352203BD8A98419 CRC64;
MITSSIAKLD LHAFKGVFCP SITVSKDDGS IDYNLWAKHL DHLIDAGING ILIFGSIGEF
YAYPLSIKKE AAKFAIEHVN HRVPVLIGVG NTNLNEVLDF TKFAESCGAD AVVAVSPYYF
GPTAPTAERY FGAIANATSL PVILYNFPAR TGSDLTPSLV ASLAEKYPNI VGIKDTVDTI
SHTRAMIEAT RRVNPDFVVF SGFDEYYTPN RIAGGNGVIC GLTNVEPETF ASLHKAYEAG
DFAHLIECAK RISHLMAVYN TTDLFISAIK AAVNLKGLPI STLVREPASQ VNSEQIEAIR
ALLK
//
