ID   ORD_ACESD               Reviewed;         353 AA.
AC   E3PY99;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=2,4-diaminopentanoate dehydrogenase {ECO:0000303|PubMed:4684685};
DE            Short=DAPDH {ECO:0000303|PubMed:4684685};
DE            EC=1.4.1.12 {ECO:0000269|PubMed:4684685};
GN   Name=ord {ECO:0000250|UniProtKB:C1FW05};
GN   OrderedLocusNames=CLOST_1294 {ECO:0000312|EMBL:CBH21414.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=4684685; DOI=10.1016/s0021-9258(19)44384-6;
RA   Somack R., Costilow R.N.;
RT   "2,4-diaminopentanoic acid C 4 dehydrogenase. Purification and properties
RT   of the protein.";
RL   J. Biol. Chem. 248:385-388(1973).
CC   -!- FUNCTION: Involved in the ornithine fermentation pathway. Catalyzes the
CC       oxidative deamination of (2R,4S)-2,4-diaminopentanoate (DAP) to yield
CC       2-amino-4-ketopentanoate (AKP). {ECO:0000305|PubMed:4684685}.
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=1.4.1.12;
CC         Evidence={ECO:0000269|PubMed:4684685};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,4S)-2,4-diaminopentanoate + H2O + NADP(+) = (2R)-2-amino-
CC         4-oxopentanoate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:24192,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58697,
CC         ChEBI:CHEBI:134102; EC=1.4.1.12;
CC         Evidence={ECO:0000269|PubMed:4684685};
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate, iodoacetate
CC       and N-ethylmaleimide. {ECO:0000269|PubMed:4684685}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:4684685}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000305}.
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DR   EMBL; FP565809; CBH21414.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PY99; -.
DR   SMR; E3PY99; -.
DR   STRING; 1511.CLOST_1294; -.
DR   EnsemblBacteria; CBH21414; CBH21414; CLOST_1294.
DR   KEGG; cst:CLOST_1294; -.
DR   eggNOG; COG3804; Bacteria.
DR   HOGENOM; CLU_050509_1_1_9; -.
DR   OMA; WGFGAMG; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0047530; F:2,4-diaminopentanoate dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0006591; P:ornithine metabolic process; TAS:UniProtKB.
DR   InterPro; IPR045760; DAP_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF19328; DAP_DH_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..353
FT                   /note="2,4-diaminopentanoate dehydrogenase"
FT                   /id="PRO_0000438116"
SQ   SEQUENCE   353 AA;  37896 MW;  E76AB2C8800AD45A CRC64;
     MEKVKVIIMG LGAMGGGMAD MLLKKQGVEI VGVVGRGKML GTSMYDHIST PRGDREDVIV
     GAMEDVITEK AADVVLLCTD SFTRKAFDKI KFIVEKKINV ISSAEEMAYP MAQEPELAKE
     IDRLAKENGV SVLGTGINPG LIMDLLVILM TGCCEEVHSI LSRRVNSLSP FGPAVMEEQG
     IGITVEEFNK GVQEGTLAGH VGFHESIGMI ADAIGWKLSA PITQSMEPIV TDVDRKSPYG
     FAKAGNVAGC AMKGFGYVDG ELKIEMDHPQ QIEPEQVGVQ TGDYVIINGV PNINMVNSPE
     VPGGIGTIAM CVNMIPQIIN ARPGLHTMID LPVPRAIMGD FRDLISEEAK IVK