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Database: UniProt
Entry: W9GT60_9PROT
LinkDB: W9GT60_9PROT
Original site: W9GT60_9PROT 
ID   W9GT60_9PROT            Unreviewed;       308 AA.
AC   W9GT60;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:EWY35871.1};
GN   ORFNames=N825_32545 {ECO:0000313|EMBL:EWY35871.1};
OS   Skermanella stibiiresistens SB22.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Skermanella.
OX   NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY35871.1, ECO:0000313|Proteomes:UP000019486};
RN   [1] {ECO:0000313|EMBL:EWY35871.1, ECO:0000313|Proteomes:UP000019486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB22 {ECO:0000313|EMBL:EWY35871.1,
RC   ECO:0000313|Proteomes:UP000019486};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Skermanella stibiiresistens.";
RL   Submitted (AUG-2013) 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:EWY35871.1}.
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DR   EMBL; AVFL01000063; EWY35871.1; -; Genomic_DNA.
DR   RefSeq; WP_037461783.1; NZ_AVFL01000063.1.
DR   AlphaFoldDB; W9GT60; -.
DR   STRING; 1385369.N825_32545; -.
DR   PATRIC; fig|1385369.3.peg.7082; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000019486; 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   PANTHER; PTHR12128:SF19; 5-DEHYDRO-4-DEOXYGLUCARATE DEHYDRATASE 2-RELATED; 1.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019486}.
FT   ACT_SITE        141
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         53
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   308 AA;  32588 MW;  8B010B303EFD8BD5 CRC64;
     MGEHDLKRTL TGISGILVTP FDSDDELAPK LQAPIVDRAI EAGVQILVAN GNTGEFYALT
     TDEAQTMVHA SARHIDGRVP LIAGVGRGIR NACRLAKASA EAGADALMIH QPPDPFVAPR
     GVVEYVKRVS DASGGLPLVI YLRNDGIGVK GIVELCAVEG VVGVKWATPN PLKLAEAMAA
     CDPDIVWVGG LAEVWAPPLY AVGARGFTSG LINVWPERSV AIHAALEAGD YAEARHLIAG
     MRAFEDIRAQ EMNGTNVTGV KAALRLLGHD CGRTRPPSAW PLTDTQSKML AEFVETNGLQ
     RLGPAANR
//
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