ID D3P2I0_AZOS1 Unreviewed; 300 AA.
AC D3P2I0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:BAI75000.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:BAI75000.1};
GN Name=dapA {ECO:0000313|EMBL:BAI75000.1};
GN OrderedLocusNames=AZL_b03370 {ECO:0000313|EMBL:BAI75000.1};
OS Azospirillum sp. (strain B510).
OG Plasmid pAB510b {ECO:0000313|EMBL:BAI75000.1,
OG ECO:0000313|Proteomes:UP000002040}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75000.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI75000.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI75000.1,
RC ECO:0000313|Proteomes:UP000002040};
RC PLASMID=pAB510b {ECO:0000313|EMBL:BAI75000.1};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; AP010948; BAI75000.1; -; Genomic_DNA.
DR RefSeq; WP_012976848.1; NC_013856.1.
DR AlphaFoldDB; D3P2I0; -.
DR KEGG; azl:AZL_b03370; -.
DR HOGENOM; CLU_049343_5_1_5; -.
DR OrthoDB; 7431780at2; -.
DR Proteomes; UP000002040; Plasmid pAB510b.
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 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 Plasmid {ECO:0000313|EMBL:BAI75000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
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 211
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 300 AA; 31420 MW; 3AE3EC6A60D50481 CRC64;
MSKTSGSKIG GPFVAIVTPF DGDERVEIAA LRRQVKRQAS AGNGVFCAGT NGEFYALSFD
EKLAVAEICV EAAAGQVPVL AHIGEISTHQ TIALGRAIQA LGVKAVSAIT PSFIACSQAE
LIAHYLRVAD ALTVPLYLYN IPARTGNTLE PETARVLADH PNIIGIKDSA GSQESLDGFL
AIARERGDFD VLVGPDSLVL HGLRNGAAGC ISGLGNIAPV TLNGIHAAFV AGDAAAAEAH
QTHFSTLRKE LYALGFPPAM VKRALYRAMP EVGLSRAPVL IANEADNRIK ELAARYAEAV
//