DAPAT_DESPS
ID DAPAT_DESPS Reviewed; 408 AA.
AC Q6AL81;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642};
DE Short=DAP-AT {ECO:0000255|HAMAP-Rule:MF_01642};
DE Short=DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642};
DE Short=LL-DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642};
DE EC=2.6.1.83 {ECO:0000255|HAMAP-Rule:MF_01642};
GN Name=dapL {ECO:0000255|HAMAP-Rule:MF_01642}; OrderedLocusNames=DP2165;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
CC -!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or
CC DL-DAP), required for both lysine and peptidoglycan biosynthesis.
CC Catalyzes the direct conversion of tetrahydrodipicolinate to LL-
CC diaminopimelate. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate;
CC Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57609; EC=2.6.1.83; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01642};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01642};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (aminotransferase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01642}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG36894.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG36894.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR522870; CAG36894.1; ALT_SEQ; Genomic_DNA.
DR STRING; 177439.DP2165; -.
DR EnsemblBacteria; CAG36894; CAG36894; DP2165.
DR KEGG; dps:DP2165; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_051433_0_0_7; -.
DR OMA; DFQARGC; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01642; DapL_aminotrans_1; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR019942; DapL/ALD1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43144; PTHR43144; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..408
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000342234"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 132
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 245..247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 291
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ SEQUENCE 408 AA; 45078 MW; AFBED49B2D6F5603 CRC64;
MITINENYLK LQASYLFSDI AKRVATFQEE NPEKEVIKLG IGDVTRGLTP SVIAAFHQAV
DEMANDSTFH GYGPEQGYAF LREAIAENDF QSRGAGIVAD EIFVSDGAKC DTSNIQEIFS
AETKIAIPDP VYPVYLDTNV MAGRTGLFAD GRYQNIVYLD STKENNFVPE LPTEKVDLIY
LCFPNNPTGS TITKAGLKRW VDYAIENKAL ILFDAAYEAF IQDDTLPKSI YEIEGADKVA
IEFRSFSKNA GFTGTRCAYT VVPKACMAYD SEGNSHSLHS MWNRRHCTKF NGVSYPIQRA
AAATYTPEGK AECKELIDYY MANAKVVXSN HDKLGYSYVG GENSPYIWID GKTDSWEFFD
MLLSKAGVVC TPGAGFGTCC GNGYIRISAF NSPENIEKAM ARITEALS
