GenomeNet

Database: UniProt
Entry: B0JUM0
LinkDB: B0JUM0
Original site: B0JUM0 
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-OCT-2014, entry version 47.
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=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. {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: Pyridoxal phosphate. {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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP009552; BAG04468.1; -; Genomic_DNA.
DR   RefSeq; WP_012267202.1; NC_010296.1.
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; HAPYVWL; -.
DR   OrthoDB; EOG6XWV2X; -.
DR   BioCyc; MAER449447:GHO8-4681-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;
KW   Reference proteome; Transferase.
FT   CHAIN         1    411       LL-diaminopimelate aminotransferase.
FT                                /FTId=PRO_1000088214.
FT   BINDING      42     42       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01642}.
FT   BINDING      72     72       Pyridoxal phosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING      75     75       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01642}.
FT   BINDING     109    109       Substrate. {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     215    215       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     218    218       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     246    246       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01642}.
FT   BINDING     248    248       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       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-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   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
//
DBGET integrated database retrieval system