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Database: UniProt
Entry: L1MG40_9CORY
LinkDB: L1MG40_9CORY
Original site: L1MG40_9CORY 
ID   L1MG40_9CORY            Unreviewed;       310 AA.
AC   L1MG40;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Dihydrodipicolinate synthetase family protein {ECO:0000313|EMBL:EKX90223.1};
GN   ORFNames=HMPREF9997_01438 {ECO:0000313|EMBL:EKX90223.1};
OS   Corynebacterium durum F0235.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX90223.1, ECO:0000313|Proteomes:UP000010445};
RN   [1] {ECO:0000313|EMBL:EKX90223.1, ECO:0000313|Proteomes:UP000010445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0235 {ECO:0000313|EMBL:EKX90223.1,
RC   ECO:0000313|Proteomes:UP000010445};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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:EKX90223.1}.
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DR   EMBL; AMEM01000018; EKX90223.1; -; Genomic_DNA.
DR   RefSeq; WP_006063667.1; NZ_KB290831.1.
DR   AlphaFoldDB; L1MG40; -.
DR   STRING; 1035195.HMPREF9997_01438; -.
DR   PATRIC; fig|1035195.3.peg.1293; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_5_1_11; -.
DR   OrthoDB; 3175637at2; -.
DR   Proteomes; UP000010445; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010445}.
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         212
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   310 AA;  32960 MW;  5C8B696696929C31 CRC64;
     MSVSAYTGVI PPVVTPFNED FSIDRESLAT QVRRMIDAGV DGLFALGSSA EVAFLTRENR
     RAVIETIVKA ADGKVPVLVG VIDTTTLRVA EHVADAVELG ASGLVATAPF YVRTHPNEIL
     NHFRLIHEMA PELPLYLYQI PVSVHVTVSD DLILQLAEEG VIAGLKDSSG LDGATRALIE
     KRNARNLTNF KVLTGSETTV DLNYFFGADG VVPGLGNVDP AGYVRLAAAC TAGDWDAARA
     EQQRLNKLFQ IVFVGDGARM GGSSAGLGGF KAALQHLGVF TSGRMAPPHV ALNDEELATI
     HSIVDQADLN
//
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