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Database: UniProt
Entry: A0A061DTV2_THECC
LinkDB: A0A061DTV2_THECC
Original site: A0A061DTV2_THECC 
ID   A0A061DTV2_THECC        Unreviewed;       366 AA.
AC   A0A061DTV2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE            EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
GN   ORFNames=TCM_005490 {ECO:0000313|EMBL:EOX96184.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX96184.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX96184.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC       {ECO:0000256|ARBA:ARBA00003294}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC         Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000594};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00005120}.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|ARBA:ARBA00007592}.
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DR   EMBL; CM001879; EOX96184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DTV2; -.
DR   STRING; 3641.A0A061DTV2; -.
DR   EnsemblPlants; EOX96184; EOX96184; TCM_005490.
DR   Gramene; EOX96184; EOX96184; TCM_005490.
DR   eggNOG; ENOG502QQ8M; Eukaryota.
DR   InParanoid; A0A061DTV2; -.
DR   OMA; DYLINMQ; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000026915; Chromosome 1.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00950; DHDPS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005263; DapA.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   NCBIfam; TIGR00674; dapA; 1.
DR   PANTHER; PTHR12128:SF15; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00665; DHDPS_1; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ   SEQUENCE   366 AA;  40327 MW;  F7B789225EE39703 CRC64;
     MATLKSYGVR LGESTHQFPL PNRGDNYKSR RNAKWRSPQA AVIPNFHLPM RSFEVKNRTS
     SEDIKSLRLI TAIKTPYLPD GRFDLEAYDG LVNMQIENGA EGVIVGGTTG EGQLMSWDEH
     IMLIGHTVNC FGGSIKVIGN TGSNSTREAI HATEQGFAVG MHAALHINPY YGKTSLEGLV
     SHFDSVLPMG PTIIYNVPSR TGQDIPPRVI NTVAQSPNLA GVKECVGNDR IEQYTDNGIV
     VWSGNDDQCH DARWSHGATG VISVTSNLIP GLMRELMFGG KNPSLNVKLL PLIEWLFEEP
     NPIGLNTALA QLGVVRPVFR LPYVPLPLAK RVEFVNLVRQ IGRQNFVGEK DVQVLDNDDF
     ILVGRY
//
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