ID A0A0F5PE78_9SPHN Unreviewed; 299 AA.
AC A0A0F5PE78;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:KKC25859.1};
GN ORFNames=WP12_11760 {ECO:0000313|EMBL:KKC25859.1};
OS Sphingomonas sp. SRS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC25859.1, ECO:0000313|Proteomes:UP000033680};
RN [1] {ECO:0000313|EMBL:KKC25859.1, ECO:0000313|Proteomes:UP000033680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS2 {ECO:0000313|EMBL:KKC25859.1,
RC ECO:0000313|Proteomes:UP000033680};
RA Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT isolated from an agricultural field in the United Kingdom.";
RL Submitted (MAR-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:KKC25859.1}.
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DR EMBL; LARW01000088; KKC25859.1; -; Genomic_DNA.
DR RefSeq; WP_046193909.1; NZ_LARW01000088.1.
DR AlphaFoldDB; A0A0F5PE78; -.
DR STRING; 133190.WP12_11760; -.
DR PATRIC; fig|133190.4.peg.4241; -.
DR OrthoDB; 9778880at2; -.
DR Proteomes; UP000033680; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000033680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 50
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 208
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 299 AA; 31797 MW; 1C8F4840B45387DF CRC64;
MTSLRLPHGI YPYLVSPTDD EGRIDTAVLA RLVDDLIHAG VDGLTPLGST GEVIYLTQEQ
RRQVVETTLE AAAGRVPVVP GVAAFSIEDG VQQARTWQDL GAAGIVVMRQ NGFATSEEGA
LTYFERIADA VSIPVVLYTN PALLGTDFTT AGLLRLAERP NIRYIKDATG DTGRILSLLN
HVGDKLEIFS ASAHIPAIVF LLGGVGWMAG PACVIPRAAK KLRDLVLAGD IDAALELQRT
LWPINEAFRK YPLAACIKTA LKLRGYAVGS PIAPQQPLGA DAEREIEQAL AAADAAVAP
//
