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Database: UniProt
Entry: D8SEQ0_SELML
LinkDB: D8SEQ0_SELML
Original site: D8SEQ0_SELML 
ID   D8SEQ0_SELML            Unreviewed;       368 AA.
AC   D8SEQ0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE            EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
GN   ORFNames=SELMODRAFT_179125 {ECO:0000313|EMBL:EFJ17013.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ17013.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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; GL377616; EFJ17013.1; -; Genomic_DNA.
DR   RefSeq; XP_002981920.1; XM_002981874.1.
DR   AlphaFoldDB; D8SEQ0; -.
DR   STRING; 88036.D8SEQ0; -.
DR   EnsemblPlants; EFJ17013; EFJ17013; SELMODRAFT_179125.
DR   GeneID; 9633933; -.
DR   Gramene; EFJ17013; EFJ17013; SELMODRAFT_179125.
DR   KEGG; smo:SELMODRAFT_179125; -.
DR   eggNOG; ENOG502QQ8M; Eukaryota.
DR   HOGENOM; CLU_049343_3_0_1; -.
DR   InParanoid; D8SEQ0; -.
DR   OMA; ALCAMIT; -.
DR   OrthoDB; 1780992at2759; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
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   HAMAP; MF_00418; DapA; 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:UP000001514};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ   SEQUENCE   368 AA;  40780 MW;  B8546DC93E2444FD CRC64;
     MPEIRTQECR ALASSALCGT LGRAPRSAAR CGSRRACLQI RAAVMQSTPL PMRSNELKNS
     TPVEEMKKLR LISAIKTPYL PDGRFDLEAY DSLVRTQVDH GVEGLIVGGT TGEGHLMNWD
     EHIMLIAHTV NCFGDKIKVI GNTGSNSTRE AIHATEQGFA AGMHAALHIN PYYGKTSMDG
     LLLHFKSVLA MGPTVIYNVP GRTGQDIPPS VIEKIASSPN FLGVKECMGN ERVKHYTEQG
     IAVWSGNDDQ CHDSRWDFGA RGVISVVSNL VPKLMHELMF SGKNQERNEK LMPLINWLFV
     EPNPIGLNTA LSQLGLIRPV FRLPYAPLNV EKRQEFVKIV EGIGRENFPG CTEVRLLKDD
     DFLLVERY
//
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