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Database: UniProt
Entry: A0A0E4GAE1_9FIRM
LinkDB: A0A0E4GAE1_9FIRM
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ID   A0A0E4GAE1_9FIRM        Unreviewed;       301 AA.
AC   A0A0E4GAE1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=1200 {ECO:0000313|EMBL:CFX43380.1};
OS   Syntrophomonas zehnderi OL-4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX43380.1, ECO:0000313|Proteomes:UP000045545};
RN   [1] {ECO:0000313|EMBL:CFX43380.1, ECO:0000313|Proteomes:UP000045545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL-4 {ECO:0000313|EMBL:CFX43380.1,
RC   ECO:0000313|Proteomes:UP000045545};
RA   Murphy D.;
RL   Submitted (MAR-2015) 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; CGIH01000021; CFX43380.1; -; Genomic_DNA.
DR   RefSeq; WP_046496603.1; NZ_CGIH01000021.1.
DR   AlphaFoldDB; A0A0E4GAE1; -.
DR   STRING; 690567.1200; -.
DR   OrthoDB; 9779394at2; -.
DR   UniPathway; UPA00034; UER00026.
DR   Proteomes; UP000045545; 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; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
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   Pfam; PF01408; GFO_IDH_MocA; 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; 1.
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:UP000045545}.
FT   DOMAIN          4..88
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          122..180
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         69..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT   BINDING         92..94
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT   BINDING         121..125
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR025648-1"
SQ   SEQUENCE   301 AA;  32663 MW;  DF845C23EB37CA9D CRC64;
     MQKFKVAVLG YGNIGKFAVD AIQASPDMQL EGIVEPAAAY WEARPSALQD YNLVESLEQL
     PRVDVALLCI PSRAVPETAA QLLAQGINTV DSYDIHGQLS DLRIKLDQVA RQNDAVGIIS
     AGWDPGTDSI IRCMFEFMMP RGITYTNFGP GMSMGHSVAA KAISGVKNAL SMTIPVGTGV
     HRRMVYVQLE AGADFNKVSA DIKNDPYFAN DETIVNQVQD VNQLIDMGHA VSIERKGVSG
     LTHNQLAGYS MKVNNPALTA QIMVSAARAG LKQKPGAYTI IQIPPIDFLY GDKEEIIRRL
     V
//
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