ID A0A374TAF0_9BACT Unreviewed; 299 AA.
AC A0A374TAF0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=DXD25_12890 {ECO:0000313|EMBL:RGK26742.1};
OS Prevotella sp. TF12-30.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2292365 {ECO:0000313|EMBL:RGK26742.1, ECO:0000313|Proteomes:UP000262185};
RN [1] {ECO:0000313|EMBL:RGK26742.1, ECO:0000313|Proteomes:UP000262185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF12-30 {ECO:0000313|EMBL:RGK26742.1,
RC ECO:0000313|Proteomes:UP000262185};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RGK26742.1}.
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DR EMBL; QSQJ01000039; RGK26742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374TAF0; -.
DR UniPathway; UPA00034; UER00026.
DR Proteomes; UP000262185; Unassembled WGS sequence.
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}.
FT DOMAIN 4..86
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 120..178
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 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; 32501 MW; B4084BD2B2774F66 CRC64;
MKKFRAAVVG YGNIGKFTVE ALEAAPDFEI AGIVRRQGAK DKPAELANYE VVDDITKLKD
VDVAILATPT RSCPEYAEKI VALGINTVDS FDIHTGILDY RTKQMENCKK AGKVSVISAG
WDPGSDSIVR VLMESLAPKG LTYTNFGPGM SMGHSVCVRS KKGVKEALSV TIPLGEGIHR
RMVYVELEEG AKLEDVTAEI KADPYFAHDE THVFAVASVD DVKDMGHGVN LVRKGVSGKT
QNQRFEFNMS INNPALTAQV LVNVARASFR LQPGCYTMPE IPVIDMLPGT REEVVATLV
//
