GenomeNet

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   15-FEB-2017, entry version 72.
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};
GN   OrderedLocusNames=Syncc9902_2031;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01642}.
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. {ECO:0000255|HAMAP-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-
CC       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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01642}.
DR   EMBL; CP000097; ABB26989.1; -; Genomic_DNA.
DR   RefSeq; WP_011360778.1; NC_007513.1.
DR   ProteinModelPortal; Q3AW44; -.
DR   STRING; 316279.Syncc9902_2031; -.
DR   EnsemblBacteria; ABB26989; ABB26989; Syncc9902_2031.
DR   KEGG; sye:Syncc9902_2031; -.
DR   PATRIC; 23801615; VBISynSp76179_2241.
DR   eggNOG; ENOG4107QSS; Bacteria.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000223061; -.
DR   KO; K10206; -.
DR   OMA; RCAFTVV; -.
DR   OrthoDB; POG090F060R; -.
DR   UniPathway; UPA00034; UER00466.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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   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   REGION      108    109       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01642}.
FT   REGION      246    248       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01642}.
FT   BINDING      15     15       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING      42     42       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01642}.
FT   BINDING      72     72       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     132    132       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     132    132       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     187    187       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     187    187       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     218    218       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     257    257       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     292    292       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     292    292       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     388    388       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   MOD_RES     249    249       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01642}.
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
//
DBGET integrated database retrieval system