DAPAT_DEHMC
ID DAPAT_DEHMC Reviewed; 388 AA.
AC Q3ZXC8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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}; OrderedLocusNames=cbdbA714;
OS Dehalococcoides mccartyi (strain CBDB1).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=255470;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBDB1;
RX PubMed=16116419; DOI=10.1038/nbt1131;
RA Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT "Genome sequence of the chlorinated compound-respiring bacterium
RT Dehalococcoides species strain CBDB1.";
RL Nat. Biotechnol. 23:1269-1273(2005).
CC -!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or
CC DL-DAP), required for both lysine and peptidoglycan biosynthesis.
CC Catalyzes the direct conversion of tetrahydrodipicolinate to LL-
CC diaminopimelate. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate;
CC Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57609; EC=2.6.1.83; Evidence={ECO:0000255|HAMAP-
CC 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-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 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01642}.
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DR EMBL; AJ965256; CAI82875.1; -; Genomic_DNA.
DR RefSeq; WP_011309226.1; NC_007356.1.
DR AlphaFoldDB; Q3ZXC8; -.
DR SMR; Q3ZXC8; -.
DR KEGG; deh:cbdbA714; -.
DR HOGENOM; CLU_017584_4_5_0; -.
DR OMA; YPHMPTG; -.
DR UniPathway; UPA00034; UER00466.
DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; IEA:UniProtKB-UniRule.
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/ALD1.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; Pyridoxal phosphate; Transferase.
FT CHAIN 1..388
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000342230"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 101..102
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 126
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 235..237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 246
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ SEQUENCE 388 AA; 42366 MW; 12A7751C85B1DE59 CRC64;
MKLSKRIENL PPYLFVQISK KIAEKRAKGE EVISFAIGDP DLPTPKHILA ELCKAAEDPS
NHRYPETEGL PVLRKAMAEW YQKRFGVKLN PDTEVLPLIG SKEGIGHAAW CFLDPGDIAL
VPNPAYPVYA ISSQLAGAEV FNLPLNKGNN FLPNLEAIPQ NILSKAKVLW INYPNNPTGA
VAGLSFFQEV ANFAAKHNLA VCHDGPYSEI AFDGYKPVSF LEADGAKDVG IEFHSLSKSY
NMTGWRIGMA VGNAKMIDAL RRFKSNLDSG IPQAIQLMAI AALNGSQEII NQNCAIYQRR
RDRLVESLRN IGMEVTAPKA SLYIWAPVPE SYTSASFATE LLDKTGVVVT PGTGYGTAGE
GYIRLSLTVP DEQIEKGIAK LAGYKKSS
