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Database: UniProt
Entry: A0A101NRS7_9ACTN
LinkDB: A0A101NRS7_9ACTN
Original site: A0A101NRS7_9ACTN 
ID   A0A101NRS7_9ACTN        Unreviewed;       303 AA.
AC   A0A101NRS7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:KUM98188.1};
GN   ORFNames=AQI88_04180 {ECO:0000313|EMBL:KUM98188.1};
OS   Streptomyces cellostaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM98188.1, ECO:0000313|Proteomes:UP000054241};
RN   [1] {ECO:0000313|EMBL:KUM98188.1, ECO:0000313|Proteomes:UP000054241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM98188.1,
RC   ECO:0000313|Proteomes:UP000054241};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT   for the species Streptomyces cellostaticus.";
RL   Submitted (OCT-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:KUM98188.1}.
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DR   EMBL; LMWL01000006; KUM98188.1; -; Genomic_DNA.
DR   RefSeq; WP_066992040.1; NZ_KQ948016.1.
DR   AlphaFoldDB; A0A101NRS7; -.
DR   STRING; 67285.AQI88_04180; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000054241; 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:SF19; 5-DEHYDRO-4-DEOXYGLUCARATE DEHYDRATASE 2-RELATED; 1.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 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:UP000054241}.
FT   ACT_SITE        144
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        169
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         56
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   303 AA;  32430 MW;  CA01C1D6211A190B CRC64;
     MSSVTFETQR AALADVVAIP VTPFAADGSV AQDTHRALLR RLLDGGIRTL TPNGNTGEFY
     ALTPEERRLV TELTVDEAGD RSVILVGVGH DLPTATASAR HARTLGARMV MVHQPVHPYV
     SAAGWVDYHR AIAESVPELG VVPYIRNAQL SGARLAELAD HCPNVIGVKY AVPDTARFAA
     FARDAGLDRF VWVAGLAEPY APSYFSAGAT GFTSGLVNVA PAVSLNMIEA LRSGDFPAAM
     KVWEQIRRFE ELRAAHGSAD NVTVVKEALA ALGLCRRDVR PPSRQLPEDE RAEVAAIAAG
     WSL
//
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