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Database: UniProt
Entry: G4H8H5_9BACL
LinkDB: G4H8H5_9BACL
Original site: G4H8H5_9BACL 
ID   G4H8H5_9BACL            Unreviewed;       309 AA.
AC   G4H8H5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:EHB68160.1};
GN   ORFNames=PaelaDRAFT_0286 {ECO:0000313|EMBL:EHB68160.1};
OS   Paenibacillus lactis 154.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB68160.1, ECO:0000313|Proteomes:UP000003891};
RN   [1] {ECO:0000313|EMBL:EHB68160.1, ECO:0000313|Proteomes:UP000003891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=154 {ECO:0000313|EMBL:EHB68160.1,
RC   ECO:0000313|Proteomes:UP000003891};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA   Allgaier M., Woyke T.J.;
RT   "The draft genome of Paenibacillus lactis 154.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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DR   EMBL; AGIP01000001; EHB68160.1; -; Genomic_DNA.
DR   RefSeq; WP_007127462.1; NZ_AGIP01000001.1.
DR   AlphaFoldDB; G4H8H5; -.
DR   STRING; 743719.PaelaDRAFT_0286; -.
DR   PATRIC; fig|743719.3.peg.303; -.
DR   eggNOG; COG0329; Bacteria.
DR   OrthoDB; 9796205at2; -.
DR   Proteomes; UP000003891; 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: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   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365}.
FT   ACT_SITE        142
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        170
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
SQ   SEQUENCE   309 AA;  35098 MW;  40EE2CDDBCEED704 CRC64;
     MYQNITNGNW PVMLTPFTEQ NEVDYEALER LIDWYIERGA DGLFAVCQSS EMYTLTLEER
     VLIAAFVKAK TAGRVPVIAS GHVSDDFEDQ VAELNAIAET GVDAVVLITN RLAGPDESDD
     VWLANLDKLL ARIPEHVPLG LYECPAPYRR LLTPEMLKKC SDTGRFRFIK DVSCDLQLIG
     DKLKAVQGGS LKIFNANTAT LLGSYRLGAF GFSGVMANFH PELYTWLFRN WESRPEEAEE
     LSDFLSVASF IERQLYPVNA KYYLMLEGVL TNYRCRSKNH EEFSATQRLE VEQLHRLSKR
     YAQKFPISS
//
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