ID A0A1M6GV73_9BACT Unreviewed; 327 AA.
AC A0A1M6GV73;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05720471_11825 {ECO:0000313|EMBL:SHJ13784.1};
OS Fibrobacter sp. UWP2.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896216 {ECO:0000313|EMBL:SHJ13784.1, ECO:0000313|Proteomes:UP000184414};
RN [1] {ECO:0000313|EMBL:SHJ13784.1, ECO:0000313|Proteomes:UP000184414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWP2 {ECO:0000313|EMBL:SHJ13784.1,
RC ECO:0000313|Proteomes:UP000184414};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQYM01000018; SHJ13784.1; -; Genomic_DNA.
DR RefSeq; WP_073190250.1; NZ_FQYM01000018.1.
DR AlphaFoldDB; A0A1M6GV73; -.
DR STRING; 1896216.SAMN05720471_11825; -.
DR OrthoDB; 9779394at2; -.
DR UniPathway; UPA00034; UER00026.
DR Proteomes; UP000184414; 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; IPR032094; Meso-DAP_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01921; DAP-DH; 1.
DR Pfam; PF16654; DAPDH_C; 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; 2.
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 121..276
FT /note="Meso-diaminopimelate D-dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16654"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 68..71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 91..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 120..124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
SQ SEQUENCE 327 AA; 35635 MW; FC12D84004D2C67A CRC64;
MAKIAILGYG NLGRGVECAV KQAPDMELVA VFTRRDPATV KIQTAGVPVL NVSEMEAWKD
KVDLLIICGG SATDLPVLTP KYAAMFNVID SFDTHAKIPQ HFAAVDAAAK AAGKIAMISV
GWDPGMFSLN RVYAQSILPE GKDYTFWGKG VSQGHSDAVR RIKGVKNAKQ YTCPVEAALE
AVRSGSMPEL TTRQKHTRLV YVVAEEGADK AYIENAIKTM PNYFDEYDTT VNFISEEEFN
KNHSGLAHGG FVIRTGKTGM NKEHTHVIEY SLKLDSNPEF TTSVLVAYAR AALRMKANGV
TGCKTVLDVP PAYLSTLSDE ELRAHCL
//
