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Database: UniProt
Entry: A0A4Q7M105_9MICO
LinkDB: A0A4Q7M105_9MICO
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ID   A0A4Q7M105_9MICO        Unreviewed;       293 AA.
AC   A0A4Q7M105;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE            EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
GN   ORFNames=EV386_0695 {ECO:0000313|EMBL:RZS60437.1};
OS   Xylanibacterium ulmi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Xylanibacterium.
OX   NCBI_TaxID=228973 {ECO:0000313|EMBL:RZS60437.1, ECO:0000313|Proteomes:UP000293852};
RN   [1] {ECO:0000313|EMBL:RZS60437.1, ECO:0000313|Proteomes:UP000293852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16932 {ECO:0000313|EMBL:RZS60437.1,
RC   ECO:0000313|Proteomes:UP000293852};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC       {ECO:0000256|ARBA:ARBA00003294}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC         Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000594};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00005120}.
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:RZS60437.1}.
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DR   EMBL; SGWX01000001; RZS60437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q7M105; -.
DR   OrthoDB; 3175637at2; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000293852; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00408; DHDPS-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005263; DapA.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   NCBIfam; TIGR00674; dapA; 1.
DR   PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR   PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000293852};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
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         206
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   293 AA;  30752 MW;  782149F91DAFFAF3 CRC64;
     MFTPQGVIPA LVTPLDEDGN LLEGNLRTLL DHVIDGGVHG VFVLGSSGEI YGLTDAQKRR
     VVEITVEHVA ARVPVYAGAS EITTRDCVAT ARMAADVGGV AALSVLTPYF MTPTQSELVT
     HFTAIAAATD LPILLYNNPG RTKVGLTVPT VQRLAEIDTI VGVKDSAGDM SLTADLIRET
     PADFKVLIGK DTLIYAGLCH GADGAIASTA NIAPRLVADI YEAYQRGDLA GALDLQGRLT
     PLRSLVDVAT FPVVIKEALR MLGVDAGVCL APARELAPAH REALAEVVRA LPA
//
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