ID A0A5R9M2Q4_9ACTN Unreviewed; 304 AA.
AC A0A5R9M2Q4;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:QNA74573.1};
GN ORFNames=C8250_024130 {ECO:0000313|EMBL:QNA74573.1};
OS Streptomyces sp. So13.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2136173 {ECO:0000313|EMBL:QNA74573.1, ECO:0000313|Proteomes:UP000310490};
RN [1] {ECO:0000313|EMBL:QNA74573.1, ECO:0000313|Proteomes:UP000310490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So13.3 {ECO:0000313|EMBL:QNA74573.1,
RC ECO:0000313|Proteomes:UP000310490};
RX PubMed=31097761; DOI=.1038/s41598-019-43960-7;
RA Nunez-Montero K., Lamilla C., Abanto M., Maruyama F., Jorquera M.A.,
RA Santos A., Martinez-Urtaza J., Barrientos L.;
RT "Antarctic Streptomyces fildesensis So13.3 strain as a promising source for
RT antimicrobials discovery.";
RL Sci. Rep. 9:7488-7488(2019).
RN [2] {ECO:0000313|EMBL:QNA74573.1, ECO:0000313|Proteomes:UP000310490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So13.3 {ECO:0000313|EMBL:QNA74573.1,
RC ECO:0000313|Proteomes:UP000310490};
RX PubMed=32349314;
RA Nunez-Montero K., Quezada-Solis D., Khalil Z.G., Capon R.J., Andreote F.D.,
RA Barrientos L.;
RT "Genomic and Metabolomic Analysis of Antarctic Bacteria Revealed Culture
RT and Elicitation Conditions for the Production of Antimicrobial Compounds.";
RL Biomolecules 10:E673-E673(2020).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP048835; QNA74573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9M2Q4; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000310490; Chromosome.
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 InterPro; IPR020625; Schiff_base-form_aldolases_AS.
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.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000310490};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 167
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 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 304 AA; 30627 MW; 0F42E7E90CADCB5B CRC64;
MDLDRPLGGI HVPLITPFDA DGTVAAAALE GLAHSALDGG AAGLVALGTT AEAATLDAEE
RGTVTAIVGR VCRERGAWLT VGAGSNDTRR SGAELRALAG TEAAAALVPV PYFTRPSEAG
VVAHVEALAA DSPVPLIIYN IPYRTGQTLG IEALLRLAAI PGVVGVKHAV GGIDQDTVAL
LGAELPGFAV LAGDDVFAPA LLALGAAGAV LASAHLLTER WVELARTGDR ALGHRLAALA
AAVFAEPNPT VIKAVLHAHG RIPGPGVRLP LLPAGGPSLE TALRAWDAAG DTRVRTHALI
GEAS
//
