GenomeNet

Database: UniProt
Entry: A0A0L9U027_PHAAN
LinkDB: A0A0L9U027_PHAAN
Original site: A0A0L9U027_PHAAN 
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
//
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