ID DAPAT_MICAN Reviewed; 411 AA.
AC B0JUM0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
DE RecName: Full=LL-diaminopimelate aminotransferase;
DE Short=DAP-AT;
DE Short=DAP-aminotransferase;
DE Short=LL-DAP-aminotransferase;
DE EC=2.6.1.83;
GN Name=dapL; OrderedLocusNames=MAE_46460;
OS Microcystis aeruginosa (strain NIES-843).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M.,
RA Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S.,
RA Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
CC -!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP
CC or DL-DAP), required for both lysine and peptidoglycan
CC biosynthesis. Catalyzes the direct conversion of
CC tetrahydrodipicolinate to LL-diaminopimelate, a reaction that
CC requires three enzymes in E.coli (By similarity).
CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate + 2-oxoglutarate =
CC (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate +
CC H(2)O.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
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.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. LL-diaminopimelate aminotransferase
CC subfamily.
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DR EMBL; AP009552; BAG04468.1; -; Genomic_DNA.
DR RefSeq; YP_001659660.1; NC_010296.1.
DR ProteinModelPortal; B0JUM0; -.
DR STRING; 449447.MAE_46460; -.
DR PaxDb; B0JUM0; -.
DR PRIDE; B0JUM0; -.
DR EnsemblBacteria; BAG04468; BAG04468; MAE_46460.
DR GeneID; 5865477; -.
DR KEGG; mar:MAE_46460; -.
DR PATRIC; 22633833; VBIMicAer59304_4226.
DR eggNOG; COG0436; -.
DR HOGENOM; HOG000223061; -.
DR KO; K10206; -.
DR OMA; QDFQARG; -.
DR ProtClustDB; PRK07590; -.
DR BioCyc; MAER449447:GHO8-4681-MONOMER; -.
DR UniPathway; UPA00034; UER00466.
DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; IEA:HAMAP.
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; DAP_NH2Trfase_plant/Chlamydia.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR PANTHER; PTHR11751:SF22; PTHR11751:SF22; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR03542; DAPAT_plant; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; FALSE_NEG.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
FT CHAIN 1 411 LL-diaminopimelate aminotransferase.
FT /FTId=PRO_1000088214.
FT BINDING 42 42 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 72 72 Pyridoxal phosphate; shared with dimeric
FT partner (By similarity).
FT BINDING 75 75 Substrate; shared with dimeric partner
FT (By similarity).
FT BINDING 109 109 Substrate (By similarity).
FT BINDING 132 132 Substrate (By similarity).
FT BINDING 187 187 Pyridoxal phosphate (By similarity).
FT BINDING 187 187 Substrate (By similarity).
FT BINDING 215 215 Pyridoxal phosphate (By similarity).
FT BINDING 218 218 Pyridoxal phosphate (By similarity).
FT BINDING 246 246 Pyridoxal phosphate (By similarity).
FT BINDING 248 248 Pyridoxal phosphate (By similarity).
FT BINDING 257 257 Pyridoxal phosphate (By similarity).
FT BINDING 292 292 Substrate; shared with dimeric partner
FT (By similarity).
FT BINDING 388 388 Substrate (By similarity).
FT MOD_RES 249 249 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 411 AA; 44902 MW; 530C427968337DAB CRC64;
MATINSNYLK LKAGYLFPEI ARRVQAFAAA NPDANIIRLG IGDVTEPLPL ACREAMIKAV
EEMGDRSSFK GYGPEQGYAW LREKIAVHDF QARGCEISAD EIFISDGSKC DTGNILDIFG
DNNSIAVTDP VYPVYVDTNV MAGHTGEAND RGEYEGLIYL PITAENNFTA QIPAEKVDLI
YLCFPNNPTG ATATKEHLTA WVNYARANGS IIFFDAAYEA FITDASLPHS IYEIEGARQC
AIEFRSFSKN AGFTGTRCAL TVVPQSLTAK AADGSDVQLW KLWNRRQSTK FNGVSYIVQR
GAEAVYSPEG QAQVEELVKF YLQNATIIRE KLTAAGLEVH GGVNAPYVWV KTPQGLSSWD
FFDKLLHTCN VVGTPGSGFG AAGEGYFRLS AFNSRANVEA AMERIISKFP G
//
