DAPT2_TRIV2
ID DAPT2_TRIV2 Reviewed; 390 AA.
AC Q3MDN5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=LL-diaminopimelate aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01642};
DE Short=DAP-AT 2 {ECO:0000255|HAMAP-Rule:MF_01642};
DE Short=DAP-aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01642};
DE Short=LL-DAP-aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01642};
DE EC=2.6.1.83 {ECO:0000255|HAMAP-Rule:MF_01642};
GN Name=dapL2 {ECO:0000255|HAMAP-Rule:MF_01642}; OrderedLocusNames=Ava_1277;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA20901.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MDN5; -.
DR SMR; Q3MDN5; -.
DR STRING; 240292.Ava_1277; -.
DR EnsemblBacteria; ABA20901; ABA20901; Ava_1277.
DR KEGG; ava:Ava_1277; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_3; -.
DR OMA; LCHDHAY; -.
DR BRENDA; 2.6.1.83; 322.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000002533; 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; 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 PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..390
FT /note="LL-diaminopimelate aminotransferase 2"
FT /id="PRO_0000342211"
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 67
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 102..103
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 127
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 177
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 236..238
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ SEQUENCE 390 AA; 43399 MW; 01A42F3918DDE164 CRC64;
MQFAKRLEKI PPYLFAEINR KREALIAQGV DIINIGVGDP DKPTPAHILQ AMREAIDEAS
NHNYPPYEGT QEFREAAVKW MERRFGVVDL NPNTEVVSSI GSKEAIHNTF LAFVEAGDYT
LIPDPGYPVY RTSTIFAGGE PFTMPLKAEN KFLPDLDLIP EEVARKAKML WVNYPNNPTG
ALATLEFFEE LVAFCQQHSI LLCHDHAYSE MAYDGYKPPS VLQIPGAKDI AIEFHSLSKS
YNMTGWRIGF AVGNAYAIQG LSQVKTNVDS GVFKAIQKAA IAAYNTDEVE LQAVMSVYQN
RRDIIVKGLQ SLGWPIEPPK ATLYVWVPVP PGYTSTEFTT LLLDKCGIVV PPGVGYGVSG
EGYFRIALTI CEERLHEAIQ RMQDAGIRYS
