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Database: UniProt
Entry: A0A3N2NV44_9ACTN
LinkDB: A0A3N2NV44_9ACTN
Original site: A0A3N2NV44_9ACTN 
ID   A0A3N2NV44_9ACTN        Unreviewed;       309 AA.
AC   A0A3N2NV44;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:ROT26327.1};
GN   ORFNames=EF879_25595 {ECO:0000313|EMBL:ROT26327.1};
OS   Micromonospora sp. HM5-17.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2487710 {ECO:0000313|EMBL:ROT26327.1, ECO:0000313|Proteomes:UP000281230};
RN   [1] {ECO:0000313|EMBL:ROT26327.1, ECO:0000313|Proteomes:UP000281230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM5-17 {ECO:0000313|EMBL:ROT26327.1,
RC   ECO:0000313|Proteomes:UP000281230};
RA   Thawai C.;
RT   "Micromonospora sp. HM5-17, a new actinomycetes isolated from a hot spring
RT   soil.";
RL   Submitted (NOV-2018) 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:ROT26327.1}.
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DR   EMBL; RJWA01000014; ROT26327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2NV44; -.
DR   OrthoDB; 3175637at2; -.
DR   Proteomes; UP000281230; 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:UP000281230};
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         49
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         212
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   309 AA;  32341 MW;  3E85F1FBAEAC7267 CRC64;
     MTLAPLSGVI PPVCTPLTPD YEVDTGSLTR LVDHLLDGGV DALFVLGSTS EVAFLPDGHR
     RVVLETVVGH VAGQVPVLAG VIDMTTLRVL EHARVAAEVG VDGIVATAPF YARTHPVEIA
     GHFRTVAQRS GLPLYAYDLP ISVHSKLGAD LVLELAAEGV LTGLKDSSGD EGGLRSVILG
     RRERLADRSF AVLTGGELTV DSALWMGADG VVPGLGNVDP HGYTRLCRAA ANGDWPTARA
     EQERLVRLFE FVRVGGTRMG GSSSALGAFK AALHLRGIID HPTTAAPQTP LNAEEIAQVG
     KYLAAAGLL
//
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