GenomeNet

Database: UniProt
Entry: A0A1U7MRP1_9MICO
LinkDB: A0A1U7MRP1_9MICO
Original site: A0A1U7MRP1_9MICO 
ID   A0A1U7MRP1_9MICO        Unreviewed;       265 AA.
AC   A0A1U7MRP1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE            EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN   ORFNames=BJF81_14010 {ECO:0000313|EMBL:OLT21956.1};
OS   Ornithinimicrobium sp. CNJ-824.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Ornithinimicrobium.
OX   NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT21956.1, ECO:0000313|Proteomes:UP000185694};
RN   [1] {ECO:0000313|EMBL:OLT21956.1, ECO:0000313|Proteomes:UP000185694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT21956.1,
RC   ECO:0000313|Proteomes:UP000185694};
RX   PubMed=27902408; DOI=10.1099/mic.0.000386;
RA   Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA   Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT   "Sequencing rare marine actinomycete genomes reveals high density of unique
RT   natural product biosynthetic gene clusters.";
RL   Microbiology 162:2075-2086(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00036290};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-
CC         4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00036097};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00037922}.
CC   -!- SIMILARITY: Belongs to the DapB family.
CC       {ECO:0000256|ARBA:ARBA00006642}.
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:OLT21956.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MKKA01000015; OLT21956.1; -; Genomic_DNA.
DR   RefSeq; WP_075957835.1; NZ_MKKA01000015.1.
DR   AlphaFoldDB; A0A1U7MRP1; -.
DR   STRING; 1904966.BJF81_14010; -.
DR   OrthoDB; 9790352at2; -.
DR   Proteomes; UP000185694; Unassembled WGS sequence.
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:SF0; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 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:UP000185694}.
FT   DOMAIN          4..97
FT                   /note="Dihydrodipicolinate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01113"
FT   DOMAIN          100..231
FT                   /note="Dihydrodipicolinate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05173"
FT   REGION          154..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  26618 MW;  864B0C536B9351DD CRC64;
     MPLSVGLLGT GRLGSAIRAA AASQDDVEVV WAVGRGTVLD GPAPVDVAVD VSSADAVADH
     LAWARRTGTP LVVGTTGWDP VLVPADVDLP VLVAPNFSLG VALVEQLARA LGRYAAHAPS
     PVDLAVTDTH HRHKVDAPSG TAVLLREALV AGTRGDGSGG DDRGAGPHPV QTTSLRVGEV
     VGRHEVLAAS ALETITITHE AHDRAIFAAG ALTAARWLVG RPAGRWSMAD LAAEHLTTLA
     GPASTTGAAG TPPTTPGAPA PDAAA
//
DBGET integrated database retrieval system