ID I4M4U1_GARVA Unreviewed; 319 AA.
AC I4M4U1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:EIK84231.1};
GN ORFNames=CGSMWGv1500E_00820 {ECO:0000313|EMBL:EIK84231.1};
OS Gardnerella vaginalis 1500E.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=698957 {ECO:0000313|EMBL:EIK84231.1, ECO:0000313|Proteomes:UP000032875};
RN [1] {ECO:0000313|EMBL:EIK84231.1, ECO:0000313|Proteomes:UP000032875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1500E {ECO:0000313|EMBL:EIK84231.1,
RC ECO:0000313|Proteomes:UP000032875};
RX PubMed=22609915; DOI=10.1128/JB.00056-12;
RA Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT Consistent with Subspeciation into Genovars.";
RL J. Bacteriol. 194:3922-3937(2012).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIK84231.1}.
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DR EMBL; ADES01000001; EIK84231.1; -; Genomic_DNA.
DR RefSeq; WP_004126704.1; NZ_ADES01000001.1.
DR AlphaFoldDB; I4M4U1; -.
DR PATRIC; fig|698957.3.peg.162; -.
DR Proteomes; UP000032875; Unassembled WGS sequence.
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:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 319 AA; 33856 MW; 5F52B6062D0FB824 CRC64;
MTEKFHGVIP PVVTPLTADG EVDVVSFERS LNRMIDAGVD GLFTLGSSGE VAFSTDKRRR
EIIENVMRIV DGRVPVLVGC IDTETNRVIE HAKEAKELGA SAIVATAPFY ALGGMAEVER
HFRLIHEAVP DLPLFAYDIP VCVHTKLPGN LLVKLGKDGV LAGVKDSSND DVSFRFLVDD
NNKAGHPLTL LTGQEVVVDG AYMSGADGSV PGLANVEATG YVRMWKAAQA GDWATVKKEQ
DWLAALMRIV TVPSGVAGFG AGVGAFKTAM ALLGVFDTNQ MPDPVCPLKG ENVEAVAGVL
KEVGLTLAKT PQEVSDSTK
//
