ID A0A0Q5LLK4_9BURK Unreviewed; 312 AA.
AC A0A0Q5LLK4;
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 synthetase {ECO:0000313|EMBL:KQR45823.1};
GN ORFNames=ASF94_08585 {ECO:0000313|EMBL:KQR45823.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR45823.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR45823.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR45823.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR45823.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR45823.1,
RC ECO:0000313|Proteomes:UP000051403};
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:KQR45823.1}.
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DR EMBL; LMOV01000024; KQR45823.1; -; Genomic_DNA.
DR RefSeq; WP_056667674.1; NZ_LMOV01000024.1.
DR AlphaFoldDB; A0A0Q5LLK4; -.
DR STRING; 1736280.ASF94_08585; -.
DR OrthoDB; 199953at2; -.
DR Proteomes; UP000051403; 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; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128:SF38; DIHYDRODIPICOLINATE SYNTHETASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G00110); 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:UP000051403}.
FT BINDING 51
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 312 AA; 33645 MW; 5D9C4F4747C07C73 CRC64;
MPAIANYRGI IPAISCPFTP DHRIDERALR KLASWLAGHE GVVAIMTNGH TGEVFSLTPA
ERAEVTRIVA DELKGRCPVI SSIVCEGLKD AADHARAAVE AGAVALDVMP PHHWLRFGFT
SGHALQYFDA IHQAAPQADL VCHVYPAWTR ASYSSQLLAD LARLPYLQAF KVGQRDMNKY
ARDIQAIREA DASKAILTCH DEYLLASMVQ GVDGALVGFA TFIPQLIIDL WNAVKAGDLR
KAMEVQAVIT PLKDAVYGGG EPTGEAHARM KGGMYLAGVI DDATVRPPTE APSAQEMDAL
RAAVKQAGLL TR
//
