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Database: UniProt
Entry: Q3AW44
LinkDB: Q3AW44
Original site: Q3AW44 
ID   DAPAT_SYNS9             Reviewed;         408 AA.
AC   Q3AW44;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   19-FEB-2014, entry version 61.
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=Syncc9902_2031;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000097; ABB26989.1; -; Genomic_DNA.
DR   RefSeq; YP_378032.1; NC_007513.1.
DR   ProteinModelPortal; Q3AW44; -.
DR   STRING; 316279.Syncc9902_2031; -.
DR   EnsemblBacteria; ABB26989; ABB26989; Syncc9902_2031.
DR   GeneID; 3742991; -.
DR   KEGG; sye:Syncc9902_2031; -.
DR   PATRIC; 23801615; VBISynSp76179_2241.
DR   eggNOG; COG0436; -.
DR   HOGENOM; HOG000223061; -.
DR   KO; K10206; -.
DR   OMA; KCAIEFR; -.
DR   OrthoDB; EOG6XWV2X; -.
DR   ProtClustDB; PRK07590; -.
DR   BioCyc; SSP316279:GJCI-2064-MONOMER; -.
DR   UniPathway; UPA00034; UER00466.
DR   GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-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:UniProtKB-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; DapL_aminotrans.
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; SSF53383; 1.
DR   TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    408       LL-diaminopimelate aminotransferase.
FT                                /FTId=PRO_0000312547.
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   408 AA;  44315 MW;  550F10B0A89985D3 CRC64;
     MVKVNGNYLK LKAGYLFPEI GRRVKAFSAA NPEAALIRLG IGDVTEPLPL ACREAMKTAI
     DAMGTAEGFH GYGPEQGYAW LREAIAQQDF QSRGCEINAD EIFVSDGSKC DSSNILDILG
     EGNRVAVTDP VYPVYVDSNV MAGRTGDAGA EGRYAGLTYL PISADNNFSA EIPSEPVDLI
     YLCFPNNPTG AVATRAQLKA WVDYARSHNA LILFDAAYEA FIQDPEIPHS IFEIEGAREC
     AIEFRSFSKN AGFTGTRCAF TVVPKGLKGT AANGELVELW GLWNRRQSTK FNGVSYIIQR
     GAEAVYSTAG QAEVKTLVSF YMENASIIRQ ELTSLGLQIY GGEHAPYVWI KTPNGMDSWG
     FFDHLLNKAN VVGTPGSGFG AAGEGYFRLS AFNSRKNVNE AMARIKSL
//
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