ID D5EUL0_PRER2 Unreviewed; 299 AA.
AC D5EUL0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Meso-diaminopimelate D-dehydrogenase {ECO:0000256|ARBA:ARBA00021654, ECO:0000256|PIRNR:PIRNR025648};
DE Short=DAPDH {ECO:0000256|PIRNR:PIRNR025648};
DE Short=Meso-DAP dehydrogenase {ECO:0000256|PIRNR:PIRNR025648};
DE EC=1.4.1.16 {ECO:0000256|ARBA:ARBA00012080, ECO:0000256|PIRNR:PIRNR025648};
GN OrderedLocusNames=PRU_2042 {ECO:0000313|EMBL:ADE82727.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82727.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE82727.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
CC -!- FUNCTION: Catalyzes the reversible NADPH-dependent reductive amination
CC of L-2-amino-6-oxopimelate, the acyclic form of L-
CC tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-
CC diaminopimelate. {ECO:0000256|PIRNR:PIRNR025648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-
CC oxoheptanedioate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:13561,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57791, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58556; EC=1.4.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001376,
CC ECO:0000256|PIRNR:PIRNR025648};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004896, ECO:0000256|PIRNR:PIRNR025648}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR025648}.
CC -!- SIMILARITY: Belongs to the diaminopimelate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007442, ECO:0000256|PIRNR:PIRNR025648}.
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DR EMBL; CP002006; ADE82727.1; -; Genomic_DNA.
DR RefSeq; WP_013064713.1; NC_014033.1.
DR AlphaFoldDB; D5EUL0; -.
DR STRING; 264731.PRU_2042; -.
DR GeneID; 69977636; -.
DR KEGG; pru:PRU_2042; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_055796_1_0_10; -.
DR UniPathway; UPA00034; UER00026.
DR Proteomes; UP000000927; Chromosome.
DR GO; GO:0047850; F:diaminopimelate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR010190; Diaminopimelate_DH_Ddh.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR032094; Meso-DAP_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01921; DAP-DH; 1.
DR PANTHER; PTHR31873:SF6; ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF16654; DAPDH_C; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR PIRSF; PIRSF025648; DDH; 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|PIRNR:PIRNR025648};
KW Diaminopimelate biosynthesis {ECO:0000256|PIRNR:PIRNR025648};
KW Lysine biosynthesis {ECO:0000256|PIRNR:PIRNR025648};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR025648};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR025648-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR025648};
KW Reference proteome {ECO:0000313|Proteomes:UP000000927}.
FT DOMAIN 4..86
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 120..177
FT /note="Meso-diaminopimelate D-dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16654"
FT BINDING 11..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 35..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 90..92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 119..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
SQ SEQUENCE 299 AA; 32860 MW; 2D946579DBA14227 CRC64;
MKKIRAAVVG YGNIGKYALE ALETAPDFEV AGIVRRNGAE NKPAELAQYE VVKDIRDLKD
VDVAILATPT RSCEEYANQI LPLGINTVDS FDIHTQIRGY RERLMKLNKE TNTVSVIAAG
WDPGSDSIVR TLMQSLAPKG LSYTNFGPGM SMGHSVCVRS KEGVKNALSM TIPLGEGIHR
RMVYVELEEG AKLEEVTKAI KADPYFASDE THVFQVESVD DVRDMGHGVN LVRKGVSGKT
QNQRLEFNMS INNPALTGQV LVNVARASMR LQPGCYTMVE IPVIDMLPGD RADLIEHLV
//
