ID A0A0Q4Y5B2_9BURK Unreviewed; 305 AA.
AC A0A0Q4Y5B2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:KQP14255.1};
GN ORFNames=ASF43_15645 {ECO:0000313|EMBL:KQP14255.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP14255.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP14255.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14255.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP14255.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14255.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQP14255.1}.
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DR EMBL; LMMV01000022; KQP14255.1; -; Genomic_DNA.
DR RefSeq; WP_056185218.1; NZ_LMMV01000022.1.
DR AlphaFoldDB; A0A0Q4Y5B2; -.
DR STRING; 1736316.ASF43_15645; -.
DR OrthoDB; 9778880at2; -.
DR Proteomes; UP000051560; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; 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; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 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:UP000051560}.
FT ACT_SITE 144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 168
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 56
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 305 AA; 32113 MW; 951FD80BEC642137 CRC64;
MATFQGPALR QALNGISGIL VTPFDKDDRV AAAPLRPVVE RAVQAGVHVL VANGNTSEFY
GLQAAEAEQA IHIAADCVAG RVPLLAGVGR SVHEACALAR VSRAAGADAL MVHQPPDPFV
SPRGVVAYVQ AIADAGGGLP VVLYLRNENI GLAAIEALCR IPEVVGIKWA SPTPLVLAAA
MRRTADRDLA WVGGLAEVWA PPLYAVGARG FTSGLINVLP QRSVAIHDAL EAADYPLAQR
LIAEMLPFED LRAQENNGTN VTVVKTALQL MGNDCGATRA PSAWPLADAQ QQQLRALLDG
WNLLR
//
