ID   ORD_UNKP                Reviewed;         339 AA.
AC   C1FW05;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=2,4-diaminopentanoate dehydrogenase {ECO:0000303|PubMed:19251850};
DE            Short=DAPDH {ECO:0000303|PubMed:19251850};
DE            EC=1.4.1.26 {ECO:0000269|PubMed:19251850};
GN   Name=ord {ECO:0000303|PubMed:19251850};
GN   ORFNames=DIG-28672_33 {ECO:0000312|EMBL:CAQ42978.1};
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   Genoscope - CEA;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP   AND SUBUNIT.
RX   PubMed=19251850; DOI=10.1128/jb.01777-08;
RA   Fonknechten N., Perret A., Perchat N., Tricot S., Lechaplais C.,
RA   Vallenet D., Vergne C., Zaparucha A., Le Paslier D., Weissenbach J.,
RA   Salanoubat M.;
RT   "A conserved gene cluster rules anaerobic oxidative degradation of L-
RT   ornithine.";
RL   J. Bacteriol. 191:3162-3167(2009).
CC   -!- FUNCTION: Involved in the ornithine fermentation pathway. Catalyzes the
CC       oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to
CC       yield 2-amino-4-ketopentanoate (AKP). Although Ord is more efficient
CC       with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be
CC       metabolized. Ord is specific for NAD as hydrogen acceptor.
CC       {ECO:0000269|PubMed:19251850}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,4S)-2,4-diaminopentanoate + H2O + NAD(+) = (2R)-2-amino-4-
CC         oxopentanoate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:24196,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58697,
CC         ChEBI:CHEBI:134102; EC=1.4.1.26;
CC         Evidence={ECO:0000269|PubMed:19251850};
CC   -!- ACTIVITY REGULATION: Allosterically activated by (2R,4S)-DAP.
CC       Negatively regulated by AKP, and by both acetyl-CoA and D-alanine.
CC       {ECO:0000269|PubMed:19251850}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16 uM for NAD {ECO:0000269|PubMed:19251850};
CC         KM=2560 uM for NADP {ECO:0000269|PubMed:19251850};
CC         Note=kcat is 34 sec(-1) with NAD as hydrogen acceptor. kcat is 5
CC         sec(-1) with NADP as hydrogen acceptor.
CC         {ECO:0000269|PubMed:19251850};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19251850}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU695246; CAQ42978.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1FW05; -.
DR   SMR; C1FW05; -.
DR   KEGG; ag:CAQ42978; -.
DR   BioCyc; MetaCyc:DIAMINOPENDHST-MON; -.
DR   GO; GO:0047530; F:2,4-diaminopentanoate dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   GO; GO:0006591; P:ornithine metabolic process; IDA:UniProtKB.
DR   InterPro; IPR045760; DAP_DH_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF19328; DAP_DH_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..339
FT                   /note="2,4-diaminopentanoate dehydrogenase"
FT                   /id="PRO_0000438115"
SQ   SEQUENCE   339 AA;  36466 MW;  B6B7D2031752FC7E CRC64;
     MGKNVKTLIW GFGAMGSGMA SILLEKGGYE LVSVIDTHPQ KAGKDVGELL GRAPLGVKVT
     MDHLKAFGSH PDVALIATSS FVEEVSPQIE FALENDANVI TIAEEMSYPW IDSKEIAERL
     DALALNRGKT VLGTGINPGF VLDTLVVSLS GVCKEVRHIH AKRVNDLAPF GPTVMRTQGV
     GTTPEKFEEG IRSGNIVGHI GFRQSIMLIA KALGWTIEDI VEERQPIITN VRRKTNYVDV
     TPGNVAGCRH TARAYSCGRE VIFLEHPQQV CPEAEGVRTG DYVVIDGDPP VNLRIEPEIP
     GGTGTMAMAV NMIPLVVNAP PGLLTMIDLP VPRSISNGF