ID   G7GLG0_9ACTN            Unreviewed;       299 AA.
AC   G7GLG0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:GAB04435.1};
GN   Name=dapA {ECO:0000313|EMBL:GAB04435.1};
GN   ORFNames=GOAMR_19_01220 {ECO:0000313|EMBL:GAB04435.1};
OS   Gordonia amarae NBRC 15530.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB04435.1, ECO:0000313|Proteomes:UP000006023};
RN   [1] {ECO:0000313|EMBL:GAB04435.1, ECO:0000313|Proteomes:UP000006023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB04435.1,
RC   ECO:0000313|Proteomes:UP000006023};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL   Submitted (NOV-2011) 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:GAB04435.1}.
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DR   EMBL; BAED01000019; GAB04435.1; -; Genomic_DNA.
DR   RefSeq; WP_005183483.1; NZ_BAED01000019.1.
DR   AlphaFoldDB; G7GLG0; -.
DR   STRING; 1075090.GOAMR_19_01220; -.
DR   eggNOG; COG0329; Bacteria.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000006023; 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:SF74; BLL4423 PROTEIN; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006023}.
FT   ACT_SITE        136
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        164
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         205
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   299 AA;  32520 MW;  AC10A720CFAFEE8D CRC64;
     MTQQPWRGIH VATALPFNDD LSVDYDAWEQ EVVWLAENGM DGVTPNGSLG EYQTLTDTER
     AKVVQIAVDA APEGFRVMPG CGAYGALESV RWAQQAAEAG AQSILLLPPN TFRADRATVV
     DHYRRVAQVG LPIVAYNNPL DTKVDMMPDL LAELHGLGYI KAVKEFTGDP RRIYEIHELA
     PELDVLIGSD DVLLEVGLGG ATGWIAGYPN AFPNACRKLY DLATSGKPED AVAALPLYRD
     LHPLLRWDSK TEFVQAIKLS MDMVGRKGGV CRPPRSPLSP EFTAAVTKAT ENAIAAGYN
//