DAPAT_DESHD
ID DAPAT_DESHD Reviewed; 411 AA.
AC Q18T09; B8FWR7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Dhaf_4564;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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 or pyruvate as the amino-group acceptor. {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=38.2 uM for LL-2,6-diaminopimelate {ECO:0000269|PubMed:18310350};
CC KM=9.1 uM for L-2,3,4,5-tetrahydrodipicolinate
CC {ECO:0000269|PubMed:18310350};
CC KM=0.70 mM for 2-oxoglutarate {ECO:0000269|PubMed:18310350};
CC KM=10.1 mM for glutamate {ECO:0000269|PubMed:18310350};
CC Vmax=0.40 umol/min/mg enzyme for the forward reaction
CC (tetrahydrodipicolinate synthesis) {ECO:0000269|PubMed:18310350};
CC Vmax=0.007 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001336; ACL22565.1; -; Genomic_DNA.
DR RefSeq; WP_015945308.1; NC_011830.1.
DR AlphaFoldDB; Q18T09; -.
DR SMR; Q18T09; -.
DR EnsemblBacteria; ACL22565; ACL22565; Dhaf_4564.
DR KEGG; dhd:Dhaf_4564; -.
DR HOGENOM; CLU_051433_0_0_9; -.
DR OMA; DFQARGC; -.
DR BRENDA; 2.6.1.83; 1880.
DR SABIO-RK; Q18T09; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000007726; Chromosome.
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; IPR019942; DapL/ALD1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43144; PTHR43144; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..411
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000342231"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 132
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 188
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 219
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 247..249
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 258
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 293
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT MOD_RES 250
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ SEQUENCE 411 AA; 45914 MW; 3A76CC7AB6C1FDA7 CRC64;
MAQINENYLK LPGSYLFSEI ARRVNEFKVQ NPDADIIRLG IGDVTRPLAP VVVEAMKQAV
EEMGRAETFR GYGPEQGYDF LIEKIIANDY APRGVQLGMD EVFVSDGAKS DTANFQEIFG
VDNIMAVTDP VYPVYVDSNV MAGRTGNYDT EKGQYGRIIY LPCTEEGDMK PELPTAPVDM
IYLCFPNNPT GMTLTKEELK VWVDYARENK AIILFDSAYE AFIREEGVPR SIYEVEGARE
VAVEFRSFSK TAGFTGTRCA YTVVPKDIMI YDSTGEGHSL NKLWLRRQTT KFNGVSYPVQ
AGAAAVYTEE GKKQIQATID YYMENARIIR EGLQEAGFKV FGGVNAPYIW MKTPGTMGSW
EFFDKLMTEA HVVGTPGAGF GANGEGFFRL TAFGTRENTE KAIERIKARM K
