ID A0A6G4U8W7_9ACTN Unreviewed; 312 AA.
AC A0A6G4U8W7;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:NGN68170.1};
GN ORFNames=G5C51_30255 {ECO:0000313|EMBL:NGN68170.1};
OS Streptomyces coryli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1128680 {ECO:0000313|EMBL:NGN68170.1, ECO:0000313|Proteomes:UP000481583};
RN [1] {ECO:0000313|EMBL:NGN68170.1, ECO:0000313|Proteomes:UP000481583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7024 {ECO:0000313|EMBL:NGN68170.1,
RC ECO:0000313|Proteomes:UP000481583};
RA Sahin N.;
RT "Whole-genome analyses of novel actinobacteria.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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:NGN68170.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAAKZV010000186; NGN68170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G4U8W7; -.
DR Proteomes; UP000481583; 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 Reference proteome {ECO:0000313|Proteomes:UP000481583};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 213
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 312 AA; 32397 MW; 3F3A01B9842723D8 CRC64;
MSFPAPLTGV VPPLCTPLTA EGEVDTASMR SLVEHLVGAG VDGLFLLGSS GETAYLSDAQ
RRTALEAAVA AADGRVPVLA GVIDMTTARV IDQARMAKEA GADALVATAP FYTLTHPAEI
ANHFRRIRAA VDLPLFAYDI PVSVHSKLSR DTVLALAEDG TLAGLKDSSG DDASLRRLMV
QLRERGLLER FAVLTGAEMV VDCALLAGAH GVVPGLGNVD PAGYVELYRL CRDGKWAEAA
AAQDRLAALF SITDFGDADG SMSRSASALG AFKAALHLRG VIACPATAAP QLPLSDEAVK
GIRGLLEKAG LL
//
