ID H0TAA0_9BRAD Unreviewed; 314 AA.
AC H0TAA0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Putative Dihydrodipicolinate synthetase {ECO:0000313|EMBL:CCE03377.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:CCE03377.1};
GN ORFNames=BRAS3809_7300007 {ECO:0000313|EMBL:CCE03377.1};
OS Bradyrhizobium sp. STM 3809.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551936 {ECO:0000313|EMBL:CCE03377.1, ECO:0000313|Proteomes:UP000004098};
RN [1] {ECO:0000313|Proteomes:UP000004098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 3809 {ECO:0000313|Proteomes:UP000004098};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:CCE03377.1}.
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DR EMBL; CAFJ01000702; CCE03377.1; -; Genomic_DNA.
DR RefSeq; WP_008965920.1; NZ_CAFJ01000702.1.
DR AlphaFoldDB; H0TAA0; -.
DR OrthoDB; 199953at2; -.
DR Proteomes; UP000004098; Unassembled WGS sequence.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
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; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128:SF38; DIHYDRODIPICOLINATE SYNTHETASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G00110); 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|PIRNR:PIRNR001365, ECO:0000313|EMBL:CCE03377.1}.
FT BINDING 51
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 314 AA; 33638 MW; 73CF67D5C362AD71 CRC64;
MSVMTNFKGI IPAIAVPFNA DHSIDEAELT RYAAWLGKRR GIVGIMTNGH TGEVFSLTAK
ERAEVTRIVA RALTGICPTI SSVVCEGIKD GIEHALMAKE AGATALDIMP PHHWLRFGFK
REHCLDYFNA IGEATKLPLI VHVYPAWTRA SFSSELLAEL ARLDHVQAFK IGTREMNKYA
RDLKAIRAAA PHKALLTCHD EYLLASMVQG VDGALVGFAS LIPDLIHDLF AAVTAGDLKL
AMKLQSMIDP LKDAVYGAGE PTGEAHGRMK AAMQVAGVIR DATVRPPTHA PSAEEMAAIR
AAVAAAGLTV KAAA
//