ID E9SAL7_RUMAL Unreviewed; 329 AA.
AC E9SAL7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=CUS_7979 {ECO:0000313|EMBL:EGC03539.1};
OS Ruminococcus albus 8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC03539.1, ECO:0000313|Proteomes:UP000004259};
RN [1] {ECO:0000313|EMBL:EGC03539.1, ECO:0000313|Proteomes:UP000004259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:EGC03539.1,
RC ECO:0000313|Proteomes:UP000004259};
RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL Submitted (FEB-2011) 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:EGC03539.1}.
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DR EMBL; ADKM02000062; EGC03539.1; -; Genomic_DNA.
DR RefSeq; WP_002848248.1; NZ_JAJFOM010000001.1.
DR AlphaFoldDB; E9SAL7; -.
DR STRING; 246199.CUS_7979; -.
DR eggNOG; COG1712; Bacteria.
DR OrthoDB; 9779394at2; -.
DR UniPathway; UPA00034; UER00026.
DR Proteomes; UP000004259; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004259}.
FT DOMAIN 123..278
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 70..73
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 93..95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 122..126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
SQ SEQUENCE 329 AA; 35743 MW; 811EBA1767853417 CRC64;
MSNIRIGIVG YGNLGRGVEL AIRQNPDTEL AAVFTRRDPS SLKILTEGVG VYSVNDVADF
KDKIDVLILC GGSATDLPVQ TPQFAKLFNV IDSFDTHARI PEHFANVDAA AKEGGNVSVI
SVGWDPGMFS VQRLYGSCIL PDGKDYTFWG KGVSQGHSDA IRRVEGVADG KQYTVPVQAA
MDAVRNGEDP ELTTRQKHTR ECFVVAEEGA DKAKIEETIK TMPNYFSDYD TTVNFISQEE
LNEKHSGIPH GGFVFRSGKT GVNGETRHII EYSLKLGSNP EFTSSILVAY ARAAVRLQKE
GAAGCKTVFD IAPAYLSPKS GEELRASML
//
