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Database: UniProt
Entry: Q3AC10
LinkDB: Q3AC10
Original site: Q3AC10 
ID   DAPAT_CARHZ             Reviewed;         390 AA.
AC   Q3AC10;
DT   01-JUL-2008, 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=CHY_1492;
OS   Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-2901 / DSM 6008;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T.,
RA   Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB16059.1; -; Genomic_DNA.
DR   RefSeq; YP_360324.1; NC_007503.1.
DR   ProteinModelPortal; Q3AC10; -.
DR   STRING; 246194.CHY_1492; -.
DR   EnsemblBacteria; ABB16059; ABB16059; CHY_1492.
DR   GeneID; 3728171; -.
DR   KEGG; chy:CHY_1492; -.
DR   PATRIC; 21276115; VBICarHyd26463_1432.
DR   eggNOG; COG0436; -.
DR   HOGENOM; HOG000223051; -.
DR   KO; K10206; -.
DR   OMA; FYIWAPV; -.
DR   OrthoDB; EOG6W721W; -.
DR   ProtClustDB; PRK09276; -.
DR   BioCyc; CHYD246194:GJCN-1491-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; IPR019881; DAP-NH2Trfase_DapL_Desulfo.
DR   InterPro; IPR019942; DapL_aminotrans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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; TIGR03540; DapC_direct; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    390       LL-diaminopimelate aminotransferase.
FT                                /FTId=PRO_0000342217.
FT   BINDING      38     38       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING      64     64       Pyridoxal phosphate; shared with dimeric
FT                                partner (By similarity).
FT   BINDING     102    102       Substrate (By similarity).
FT   BINDING     126    126       Substrate (By similarity).
FT   BINDING     176    176       Pyridoxal phosphate (By similarity).
FT   BINDING     176    176       Substrate (By similarity).
FT   BINDING     204    204       Pyridoxal phosphate (By similarity).
FT   BINDING     207    207       Pyridoxal phosphate (By similarity).
FT   BINDING     235    235       Pyridoxal phosphate (By similarity).
FT   BINDING     237    237       Pyridoxal phosphate (By similarity).
FT   BINDING     246    246       Pyridoxal phosphate (By similarity).
FT   BINDING     364    364       Substrate (By similarity).
FT   MOD_RES     238    238       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   390 AA;  43112 MW;  1ABA54D7A14DCBA3 CRC64;
     MLEATRVRNL PPYLFARIER LIAEKKEAGV DVISLGIGDP DTPTPKHIIE ELYLAAQNPE
     NHQYPSSVGM LSYRQAVAAW YARRFGVELD PKTEVVSLLG SKEGIAHISW CYVDPGDLVL
     VPDPGYPVYE GGTILAGGTT YKMPLKPENG FLPDLDSIPE EVARKAKLMF INYPNNPTGA
     VADLGFFEKV VHFAKKYEIL VCHDAAYSEI TFDGYRAPSF LEVKGAKDVG IEFHSLSKTY
     NMTGWRIGWA VGNAKAIDAL GRLKSNIDSG VFQAIQYAGI KALEGPQDVV KELCDLYAQR
     RDLVIETLNK LGWNLSKPKG TFYIWAPVPK GFTSASFAEY LIEKAGVVIT PGNGYGTNGE
     GYFRISLTIP TSRLKEALQR IEQHLGKVEF
//
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