ID U2KC98_9PORP Unreviewed; 242 AA.
AC U2KC98;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN ORFNames=HMPREF1556_00677 {ECO:0000313|EMBL:ERJ72463.1};
OS Porphyromonas sp. oral taxon 278 str. W7784.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1227272 {ECO:0000313|EMBL:ERJ72463.1, ECO:0000313|Proteomes:UP000016628};
RN [1] {ECO:0000313|EMBL:ERJ72463.1, ECO:0000313|Proteomes:UP000016628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W7784 {ECO:0000313|EMBL:ERJ72463.1,
RC ECO:0000313|Proteomes:UP000016628};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERJ72463.1}.
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DR EMBL; AWUX01000040; ERJ72463.1; -; Genomic_DNA.
DR RefSeq; WP_021667012.1; NZ_KI259230.1.
DR AlphaFoldDB; U2KC98; -.
DR STRING; 1227272.HMPREF1556_00677; -.
DR PATRIC; fig|1227272.3.peg.569; -.
DR eggNOG; COG0289; Bacteria.
DR HOGENOM; CLU_047479_1_0_10; -.
DR OrthoDB; 9790352at2; -.
DR Proteomes; UP000016628; 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}.
FT DOMAIN 5..106
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 109..239
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
SQ SEQUENCE 242 AA; 26516 MW; BAB0DD8C84B4FCCA CRC64;
MQGLKIVLIG YGKMGHVIEK IAQARGHQIV LTIDRGEEAL FDDPRFASAD VAIEFTAPAM
AFDNCLRAIE RGIPVVSGTT GWTDRQPELR ARCEAGEGTV FWSSNFSIGV NLFLQINRRV
AALMQAAPNY HLSMDETHHI HKLDAPSGTA ITLAEAILSE RPELTGWELS EEPHTGLLPI
TAHREGEVPG IHTVTYTSEV DRIVLTHEAF GRQGFALGAV LAAEFAHTHQ GWLTMDDMLQ
LG
//
