ID   DAPAT_CROS5             Reviewed;         411 AA.
AC   B1WSG7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=cce_2605;
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(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; CP000806; ACB51953.1; -; Genomic_DNA.
DR   RefSeq; WP_009544705.1; NC_010546.1.
DR   AlphaFoldDB; B1WSG7; -.
DR   SMR; B1WSG7; -.
DR   STRING; 43989.cce_2605; -.
DR   EnsemblBacteria; ACB51953; ACB51953; cce_2605.
DR   KEGG; cyt:cce_2605; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_051433_0_0_3; -.
DR   OMA; DFQARGC; -.
DR   OrthoDB; 417859at2; -.
DR   UniPathway; UPA00034; UER00466.
DR   Proteomes; UP000001203; Chromosome circular.
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..411
FT                   /note="LL-diaminopimelate aminotransferase"
FT                   /id="PRO_1000186860"
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         187
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         218
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         246..248
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         257
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         292
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   MOD_RES         249
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ   SEQUENCE   411 AA;  45374 MW;  97CAC8BC8F6A582C CRC64;
     MATINDNYLK LKAGYLFPEI ARRVNTFIEA NPEAKIIKLG IGDVTEPLPE ACRTAMIKAV
     EDMGDRSSFK GYGPEQGYGW LREKIAAQDF QARGCDIDAS EIFVSDGAKC DTGNILDIFG
     KNNKIAVTDP VYPVYVDTNV MAGHTGETNE KGEYEGLVYL PISADNHFVA DIPSEKVDLI
     YLCFPNNPTG ATATKEYLKA WVDYATANDS IIFFDAAYEA FITDESLPHS IYEIEGAKDC
     AIEFRSFSKN AGFTGTRCAF TVVPKQLTAK ASDGSQVELW KLWNRRQSTK FNGVSYIVQR
     GAEAVYSEAG KAQIKGLVSF YLENAKIICE QLKSAGFEVY GGVNAPYIWL KTPHNLSSWD
     FFDKLLQTTH VVGTPGSGFG AAGEGYFRIS AFNSRENVEE AMKRITQAFK V