DAPDH_ACET2
ID DAPDH_ACET2 Reviewed; 334 AA.
AC A3DDX7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Meso-diaminopimelate D-dehydrogenase;
DE Short=DAPDH;
DE Short=Meso-DAP dehydrogenase;
DE EC=1.4.1.16;
GN Name=ddh; OrderedLocusNames=Cthe_0922;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RX PubMed=21616177; DOI=10.1016/j.bbapap.2011.04.019;
RA Hudson A.O., Klartag A., Gilvarg C., Dobson R.C., Marques F.G., Leustek T.;
RT "Dual diaminopimelate biosynthesis pathways in Bacteroides fragilis and
RT Clostridium thermocellum.";
RL Biochim. Biophys. Acta 1814:1162-1168(2011).
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. Probably plays a role in lysine biosynthesis. Exhibits
CC a high substrate specificity for meso-2,6-diaminopimelate (m-DAP),
CC since the activity with L,L-2,6-diaminopimelate is less than 5% of the
CC activity observed with m-DAP. Can use NAD(+) only very poorly since the
CC activity observed in the presence of NAD(+) is about 0.3% of that with
CC NADP(+). {ECO:0000269|PubMed:21616177}.
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:0000269|PubMed:21616177};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for meso-2,6-diaminoheptanedioate (at 30 degrees Celsius
CC and pH 10.5) {ECO:0000269|PubMed:21616177};
CC KM=0.13 mM for NADP(+) (at 30 degrees Celsius and pH 10.5)
CC {ECO:0000269|PubMed:21616177};
CC KM=0.09 mM for L-2-amino-6-oxoheptanedioate (at 30 degrees Celsius
CC and pH 10.5) {ECO:0000269|PubMed:21616177};
CC KM=0.21 mM for NADPH (at 30 degrees Celsius and pH 10.5)
CC {ECO:0000269|PubMed:21616177};
CC KM=195 mM for ammonia (at 30 degrees Celsius and pH 10.5)
CC {ECO:0000269|PubMed:21616177};
CC Vmax=15.45 umol/min/mg enzyme for the reductive amination of L-2-
CC amino-6-oxopimelate (at 30 degrees Celsius and pH 10.5)
CC {ECO:0000269|PubMed:21616177};
CC Vmax=0.24 umol/min/mg enzyme for the oxidative deamination of meso-
CC 2,6-diaminopimelate (at 30 degrees Celsius and pH 10.5)
CC {ECO:0000269|PubMed:21616177};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:21616177};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step
CC 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:21616177}.
CC -!- SIMILARITY: Belongs to the diaminopimelate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000568; ABN52156.1; -; Genomic_DNA.
DR AlphaFoldDB; A3DDX7; -.
DR SMR; A3DDX7; -.
DR STRING; 203119.Cthe_0922; -.
DR EnsemblBacteria; ABN52156; ABN52156; Cthe_0922.
DR KEGG; cth:Cthe_0922; -.
DR eggNOG; COG1748; Bacteria.
DR HOGENOM; CLU_055796_0_0_9; -.
DR OMA; WDPGLFS; -.
DR UniPathway; UPA00034; UER00026.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0047850; F:diaminopimelate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010190; Diaminopimelate_DH_Ddh.
DR InterPro; IPR032094; Meso-DAP_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16654; DAPDH_C; 1.
DR PIRSF; PIRSF025648; DDH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01921; DAP-DH; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Meso-diaminopimelate D-dehydrogenase"
FT /id="PRO_0000417123"
FT BINDING 16..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 40..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 75..78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 98..100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160..161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 37224 MW; 7A2E8D84A3DA542B CRC64;
MGGVTLEKIR IGIVGYGNLG KGAELGIRQN KDMELVGIFT RRNPNSIKPL TEGVKVYSVD
SARDMADKID VMLLCSGSRT DLPVQGPEFA AMFNIVDGFD THNKIQEYFE SVDAKAKESK
KVAVIACGWD PGMFSLNRLF GEVILPEGKT YTFWGKGVSQ GHSDAIRRVK GVVDAKQYTI
PVESAIELVR KGENPELTTR QKHIRECFVV VEEGADKERI EREIKTMPDY FADYDTIVHF
ISLEELKEKH SGIPHGGFSI RTGRTGINNE NKHTIEYSLK LDSNPDFTAN TLLAYARAAY
RLNKEGVFGA KTVFDIPPAY LSPKSAEELR RSLL
