DAPAT_MOOTA
ID DAPAT_MOOTA Reviewed; 390 AA.
AC Q2RK33;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:18310350};
DE Short=DAP-AT {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:18310350};
DE Short=DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:18310350};
DE Short=LL-DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:18310350};
DE EC=2.6.1.83 {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000269|PubMed:18310350};
GN Name=dapL {ECO:0000255|HAMAP-Rule:MF_01642}; OrderedLocusNames=Moth_0889;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=18310350; DOI=10.1128/jb.01381-07;
RA Hudson A.O., Gilvarg C., Leustek T.;
RT "Biochemical and phylogenetic characterization of a novel diaminopimelate
RT biosynthesis pathway in prokaryotes identifies a diverged form of LL-
RT diaminopimelate aminotransferase.";
RL J. Bacteriol. 190:3256-3263(2008).
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. Is also able to catalyze the reverse reaction in
CC vitro, i.e. the transamination of LL-diaminopimelate with 2-
CC oxoglutarate to produce tetrahydrodipicolinate and glutamate. Can also
CC use m-DAP instead of LL-DAP as the amino-group donor, and oxaloacetate
CC instead of 2-oxoglutarate as the amino-group acceptor.
CC {ECO:0000269|PubMed:18310350}.
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, ECO:0000269|PubMed:18310350};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01642};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60.4 uM for LL-2,6-diaminopimelate {ECO:0000269|PubMed:18310350};
CC KM=14 uM for L-2,3,4,5-tetrahydrodipicolinate
CC {ECO:0000269|PubMed:18310350};
CC KM=0.30 mM for 2-oxoglutarate {ECO:0000269|PubMed:18310350};
CC KM=4.2 mM for glutamate {ECO:0000269|PubMed:18310350};
CC Vmax=0.25 umol/min/mg enzyme for the forward reaction
CC (tetrahydrodipicolinate synthesis) {ECO:0000269|PubMed:18310350};
CC Vmax=0.006 umol/min/mg enzyme for the reverse reaction (LL-DAP
CC synthesis) {ECO:0000269|PubMed:18310350};
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 ECO:0000269|PubMed:18310350}.
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; CP000232; ABC19206.1; -; Genomic_DNA.
DR RefSeq; WP_011392408.1; NC_007644.1.
DR RefSeq; YP_429749.1; NC_007644.1.
DR AlphaFoldDB; Q2RK33; -.
DR SMR; Q2RK33; -.
DR STRING; 264732.Moth_0889; -.
DR EnsemblBacteria; ABC19206; ABC19206; Moth_0889.
DR GeneID; 61289574; -.
DR KEGG; mta:Moth_0889; -.
DR PATRIC; fig|264732.11.peg.956; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_9; -.
DR OMA; FYLYVEI; -.
DR BRENDA; 2.6.1.83; 1528.
DR SABIO-RK; Q2RK33; -.
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 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..390
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000342250"
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 390 AA; 43318 MW; 6500EC02D5A17860 CRC64;
MQEARRIREL PPYLFARIEK KIAEARERGV DIISLGIGDP DMPTPSHVID KLVAEAHNPE
NHRYPTSEGL LAFRQAVADW YQRLYGVDLD PRREVVTLIG SKEGIAHISL CYVDPGDINL
VPDPGYPVYN IGTLLAGGES YFMPLTAANG FLPDLGAIPS DVARRAKLMF INYPNNPTGA
VADLKFFQEV VEFARSYDLI VCHDAAYSEI TYDGYRAPSF LQAPGAKEVG IEFNSVSKPY
NMTGWRLGWA CGRADVIEAL ARIKSNIDSG AFQAVQYAGI AALTGPQEGL AEVRRVYQER
RDIIVEGFNS LGWHLEKPKA TFYVWAPVPR GYTSASFAEM VLEKAGVIIT PGNGYGNYGE
GYFRIALTIS KERMQEAIER LRRVLGKVEF
