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Database: UniProt
Entry: F3PDF3_9BACE
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Original site: F3PDF3_9BACE 
ID   F3PDF3_9BACE            Unreviewed;       254 AA.
AC   F3PDF3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE            EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN   ORFNames=HMPREF9445_00010 {ECO:0000313|EMBL:EGF55046.1};
OS   Bacteroides clarus YIT 12056.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF55046.1, ECO:0000313|Proteomes:UP000010321};
RN   [1] {ECO:0000313|EMBL:EGF55046.1, ECO:0000313|Proteomes:UP000010321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF55046.1,
RC   ECO:0000313|Proteomes:UP000010321};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:EGF55046.1}.
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DR   EMBL; AFBM01000001; EGF55046.1; -; Genomic_DNA.
DR   RefSeq; WP_009120227.1; NZ_GL882580.1.
DR   AlphaFoldDB; F3PDF3; -.
DR   STRING; 762984.SAMN05444376_2950; -.
DR   GeneID; 61677739; -.
DR   eggNOG; COG0289; Bacteria.
DR   HOGENOM; CLU_047479_1_0_10; -.
DR   OrthoDB; 9790352at2; -.
DR   Proteomes; UP000010321; 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   NCBIfam; TIGR00036; dapB; 1.
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}.
FT   DOMAIN          1..104
FT                   /note="Dihydrodipicolinate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01113"
FT   DOMAIN          107..248
FT                   /note="Dihydrodipicolinate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05173"
SQ   SEQUENCE   254 AA;  27617 MW;  E02A2738918241E4 CRC64;
     MKIALIGYGK MGKEIEKIAL SRGHEIVSII DINNQEDFES DAFKSADVAI EFTNPMVAYN
     NYMKAFKAGV KLVSGSTGWL EEHGEEVRKL CTEGGKTLFW SSNFSLGVAI FSAVNKYLAK
     IMNRFPAYDV TMSETHHIHK LDAPSGTAIT LAEGILENLD RKDRWVKGTL QAPDGSVSGS
     AECAADELPV SSIREGEVPG IHSIRYDSEA DSITITHDAK NRSGFALGAV LAAEYTAGKQ
     GFLGMSDLFP FLKD
//
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