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DAPAT_AZOPC
ID   DAPAT_AZOPC             Reviewed;         401 AA.
AC   B6YRL2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=CFPG_571;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(2008).
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}.
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DR   EMBL; AP010656; BAG83834.1; -; Genomic_DNA.
DR   RefSeq; WP_012573594.1; NC_011565.1.
DR   AlphaFoldDB; B6YRL2; -.
DR   SMR; B6YRL2; -.
DR   STRING; 511995.CFPG_571; -.
DR   EnsemblBacteria; BAG83834; BAG83834; CFPG_571.
DR   KEGG; aps:CFPG_571; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_051433_0_0_10; -.
DR   OMA; DFQARGC; -.
DR   OrthoDB; 417859at2; -.
DR   UniPathway; UPA00034; UER00466.
DR   Proteomes; UP000000723; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="LL-diaminopimelate aminotransferase"
FT                   /id="PRO_1000186859"
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         176
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         207
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         235..237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         246
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         281
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   MOD_RES         238
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ   SEQUENCE   401 AA;  44882 MW;  763EEC12BCC64EFE CRC64;
     MVRINEHYIE ISNSYLFAEI AERVNEYKQN NKNREVISLG IGDVTQAIAP AVVEAIHKAT
     NEMACTKTLR GYAPYEGYDF LIQAILKNDF TDKGISIEAD EIFVNDGAKS DTGNIGDILG
     QDNHIAITDP AYPVYVDTNR MAGRTIELLP CTPENYFVPN FPRKTADVIY LCYPNNPTGI
     ALNAAQLKNW VDYALTNKSL ILFDAAYEAY ISQQDVPHSI YEISDAKKVA IEFRSFSKTA
     GFTGLRAGYT IVPKELIIQT SKGKMLSLNA MWRRRQSTKF NGTAYIVQRG AEAVYSIEGQ
     KQIRKAIDYY RGNALTIKEG LESLGVTTYG GINAPYIWVK TPNNLTSWEF FDLLLNKIQV
     IGTPGDGFGQ AGKGFFRFTA FGNKEDTLEA VLRMKKLLEF H
 
 
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