ID A0A0S8HID7_9DELT Unreviewed; 296 AA.
AC A0A0S8HID7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:KPK85011.1};
GN ORFNames=AMJ94_19535 {ECO:0000313|EMBL:KPK85011.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK85011.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK85011.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK85011.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK85011.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJUR01000270; KPK85011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HID7; -.
DR STRING; 1703399.AMJ94_19535; -.
DR PATRIC; fig|1703399.3.peg.4402; -.
DR Proteomes; UP000051218; 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: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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365}.
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 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 296 AA; 32259 MW; 215A4DEF5E7CA2FA CRC64;
MKAKDFAGVY PYLVSPVDSR GEVMAEVLGR LVEYLIQKGV HGLTPLGSTG EFAYLTWDQR
RRVVEVVLEA SKGRVPVVAG VAHTSIREAA RQAREMEKMG VDGILAVMDT YFPVPPEGVT
AYFRAVAEAV SCPVVLYTNP SFSGTNLSPE VIESLLSTPN ILYLKDASAN TGNLLTLMNR
VGDRLKIFSA SAHIPLAVMM LGGVGWMSGP ACVIPGQSVR LYELTRRRQW DEAIALQKRL
WNINRIFQKY ALAPCIKACL EIQGFPVGPP IPPLQPLKGA ALQEIEGVLK SLQALP
//