ID A0A0L9U027_PHAAN Unreviewed; 295 AA.
AC A0A0L9U027;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dihydrodipicolinate reductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan02g215200 {ECO:0000313|EMBL:KOM36002.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM36002.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the DapB family.
CC {ECO:0000256|ARBA:ARBA00006642}.
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DR EMBL; CM003372; KOM36002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9U027; -.
DR STRING; 3914.A0A0L9U027; -.
DR EnsemblPlants; KOM36002; KOM36002; LR48_Vigan02g215200.
DR Gramene; KOM36002; KOM36002; LR48_Vigan02g215200.
DR OMA; TLCHSAH; -.
DR Proteomes; UP000053144; Chromosome 2.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022663; DapB_C.
DR InterPro; IPR000846; DapB_N.
DR InterPro; IPR023940; DHDPR_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1.
DR PANTHER; PTHR20836:SF6; DIHYDRODIPICOLINATE REDUCTASE-LIKE PROTEIN CRR1, CHLOROPLASTIC; 1.
DR Pfam; PF05173; DapB_C; 1.
DR Pfam; PF01113; DapB_N; 1.
DR PIRSF; PIRSF000161; DHPR; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 39..166
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 172..288
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
SQ SEQUENCE 295 AA; 31173 MW; 4796E2E21B34681D CRC64;
MASLSCHFHT TNLLNSKNVN SGKKKRFISC SAQPTQSNIK VVINGATKEI GRAAVVAVTK
ARGMEVAGAV DTCHVGEDIG KVCGMEEPLE IPIINDLTLI LGSISQSKAP GVVVDFTDPS
SVYENVKQAT AFGMKSIVYV PRIKLDTVAA LSALCEKATM GVLVAPTLSI GSILLQQAAI
SASFHYSNVE IVESRANAKE LPSADANQIA NNLSNIGQIY NREDSSTDVL ARGQVLGDGI
RVHSLVLPGL PSSTAVHFSG PGDVYSIKHD ITDVQCLMPG LLLAIRKVVR LKVPT
//