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Entry: I3ZJT6_TERRK
LinkDB: I3ZJT6_TERRK
Original site: I3ZJT6_TERRK 
ID   I3ZJT6_TERRK            Unreviewed;       225 AA.
AC   I3ZJT6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE            EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN   OrderedLocusNames=Terro_3287 {ECO:0000313|EMBL:AFL89504.1};
OS   Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL89504.1, ECO:0000313|Proteomes:UP000006056};
RN   [1] {ECO:0000313|EMBL:AFL89504.1, ECO:0000313|Proteomes:UP000006056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC   {ECO:0000313|Proteomes:UP000006056};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete genome of Terriglobus roseus DSM 18391.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; CP003379; AFL89504.1; -; Genomic_DNA.
DR   RefSeq; WP_014786765.1; NC_018014.1.
DR   AlphaFoldDB; I3ZJT6; -.
DR   STRING; 926566.Terro_3287; -.
DR   KEGG; trs:Terro_3287; -.
DR   PATRIC; fig|926566.3.peg.3233; -.
DR   eggNOG; COG0289; Bacteria.
DR   HOGENOM; CLU_047479_1_0_0; -.
DR   OrthoDB; 9790352at2; -.
DR   Proteomes; UP000006056; Chromosome.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; 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:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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   Oxidoreductase {ECO:0000313|EMBL:AFL89504.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006056}.
FT   DOMAIN          1..85
FT                   /note="Dihydrodipicolinate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01113"
FT   DOMAIN          108..221
FT                   /note="Dihydrodipicolinate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05173"
SQ   SEQUENCE   225 AA;  23982 MW;  717E51A0FA6E89A9 CRC64;
     MRVLVLGHGK TGKLVADVAS ERGHGVHVLD AKENPRGSAL TAPFVAGFDV VIDFTTPEAV
     LTNLRACLAV GAKVVVGTTG WYNSLHDMSA LALRKEGALL HGTNYSIGVQ VMLKIAKQMA
     EPLRKAGYEF KIEETHHVTK LDAPSGTAIS LQQALVGAGE VPITSVREGD VPGLHIVEAV
     SGADRLLLTH EAFSRRGFAE GAVRGAEWLS TRKGVYDFSD IFTEL
//
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