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Database: UniProt
Entry: D3P2I0_AZOS1
LinkDB: D3P2I0_AZOS1
Original site: D3P2I0_AZOS1 
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
//
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