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 01-MAY-2013, entry version 57.
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; HILAELC; -.
DR ProtClustDB; PRK09276; -.
DR BioCyc; CHYD246194:GJCN-1491-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; IPR019881; DAP-NH2Trfase_DapL_Desulfo.
DR InterPro; IPR019942; DAP_NH2Trfase_plant/Chlamydia.
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; PyrdxlP-dep_Trfase_major; 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
//
