ID A0A2P6SG54_ROSCH Unreviewed; 366 AA.
AC A0A2P6SG54;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
GN ORFNames=RchiOBHm_Chr1g0350811 {ECO:0000313|EMBL:PRQ57664.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ57664.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ57664.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
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}.
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:PRQ57664.1}.
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DR EMBL; PDCK01000039; PRQ57664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6SG54; -.
DR STRING; 74649.A0A2P6SG54; -.
DR EnsemblPlants; PRQ57664; PRQ57664; RchiOBHm_Chr1g0350811.
DR Gramene; PRQ57664; PRQ57664; RchiOBHm_Chr1g0350811.
DR OMA; ALCAMIT; -.
DR OrthoDB; 1780992at2759; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000238479; Chromosome 1.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:PRQ57664.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 366 AA; 40600 MW; 09362A716627D3E6 CRC64;
MASLQSCSSV CLRESALLLP RRNVNDSYKS RTVKWRSPRG AVLPNFHLPM RSFEIKNRTS
TEEIKSLRLI TAIKTPYLPD GRFDLEAYDA LVNTQIEHGA EGVIVGGTTG EGQLMSWDEH
IMLIGHTINC YGGSIKVIGN TGSNSTREAV HATEQGFAVG MHAALHINPY YGKTSLEGLV
KHFERVLSMG PTIIYNVPSR TGQDIPHQVI NTLAQNANLA GVKECVGNDR IIEHIDKGIV
VWSGNDDECH DSRWNHGATG VISVTSNLVP GLMRDLMFGG KNPSLNAKLM PLIEWLFQEP
NPIGLNTALA QLGVVRPVFR LPYVPLPYEK RVDFVNLVKQ IGREHFVGEK GVQVLDDDDF
TYLDRY
//
