ID A0A0M2XTM5_9SPHI Unreviewed; 306 AA.
AC A0A0M2XTM5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:KKO91028.1};
GN ORFNames=AAW12_12300 {ECO:0000313|EMBL:KKO91028.1};
OS Sphingobacterium sp. Ag1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO91028.1, ECO:0000313|Proteomes:UP000034524};
RN [1] {ECO:0000313|EMBL:KKO91028.1, ECO:0000313|Proteomes:UP000034524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKO91028.1,
RC ECO:0000313|Proteomes:UP000034524};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KKO91028.1}.
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DR EMBL; LBGU01000038; KKO91028.1; -; Genomic_DNA.
DR RefSeq; WP_046673939.1; NZ_LBGU01000038.1.
DR AlphaFoldDB; A0A0M2XTM5; -.
DR PATRIC; fig|1643451.3.peg.5243; -.
DR Proteomes; UP000034524; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF21; 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}.
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 171
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 213
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 306 AA; 33817 MW; CE2D66D5BD7FB751 CRC64;
MLNQKISGLI AAPFTPFDEN GELNLELIPQ YYAMLKRNRV TGAFICGSTG EGVSLTFEEK
VAVMTAWARL TKEDDAFTLM MLLGGTNIKE CQQLAGLAEQ AGVDVVSFTA PSYFKPANVD
QLAKCCVEIA RAAPNTAFYY YHIPVLTGGN FQMIDLLKQI DGVIPNFKGI KYTHEDFMDF
LSCMNYADRK YDMLWGRDEN MLSALVLGNK GAVGSTYNYA APLYLDLMEA YDKGELDKAN
ALQQQSIDMI TLLGKYGGIS VGKAYMKLIG LDCGAFRLPV KNMSVEQFEL FTEDAVKVGF
QGFCAH
//
