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LL-diaminopimelate aminotransferase 2 (DAP-AT 2) (DAP-aminotransferase 2) (LL-DAP-aminotransferase 2) (EC 2.6.1.83)

 DAPT2_ANAVT             Reviewed;         390 AA.
Q3MDN5;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
25-OCT-2017, entry version 81.
RecName: Full=LL-diaminopimelate aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01642};
Short=DAP-AT 2 {ECO:0000255|HAMAP-Rule:MF_01642};
Short=DAP-aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01642};
Short=LL-DAP-aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01642};
EC=2.6.1.83 {ECO:0000255|HAMAP-Rule:MF_01642};
Name=dapL2 {ECO:0000255|HAMAP-Rule:MF_01642};
OrderedLocusNames=Ava_1277;
Anabaena variabilis (strain ATCC 29413 / PCC 7937).
Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
NCBI_TaxID=240292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29413 / PCC 7937;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP
or DL-DAP), required for both lysine and peptidoglycan
biosynthesis. Catalyzes the direct conversion of
tetrahydrodipicolinate to LL-diaminopimelate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
-!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate + 2-oxoglutarate =
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate +
H(2)O. {ECO:0000255|HAMAP-Rule:MF_01642}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000255|HAMAP-Rule:MF_01642};
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
(aminotransferase route): step 1/1. {ECO:0000255|HAMAP-
Rule:MF_01642}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01642}.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. LL-diaminopimelate aminotransferase
subfamily. {ECO:0000255|HAMAP-Rule:MF_01642}.
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EMBL; CP000117; ABA20901.1; -; Genomic_DNA.
ProteinModelPortal; Q3MDN5; -.
SMR; Q3MDN5; -.
STRING; 240292.Ava_1277; -.
EnsemblBacteria; ABA20901; ABA20901; Ava_1277.
KEGG; ava:Ava_1277; -.
eggNOG; ENOG4105CHM; Bacteria.
eggNOG; COG0436; LUCA.
HOGENOM; HOG000223051; -.
KO; K10206; -.
OMA; LCHDHAY; -.
OrthoDB; POG091H09WQ; -.
BioCyc; AVAR240292:G7WH-8677-MONOMER; -.
BRENDA; 2.6.1.83; 322.
UniPathway; UPA00034; UER00466.
Proteomes; UP000002533; Chromosome.
GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_01642; DapL_aminotrans_1; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR019942; DapL/ALD1.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
3: Inferred from homology;
Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
CHAIN 1 390 LL-diaminopimelate aminotransferase 2.
/FTId=PRO_0000342211.
REGION 102 103 Pyridoxal phosphate binding.
{ECO:0000255|HAMAP-Rule:MF_01642}.
REGION 236 238 Pyridoxal phosphate binding.
{ECO:0000255|HAMAP-Rule:MF_01642}.
BINDING 13 13 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 38 38 Substrate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01642}.
BINDING 67 67 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 103 103 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 127 127 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 127 127 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 177 177 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 177 177 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 208 208 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 247 247 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
BINDING 365 365 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01642}.
MOD_RES 239 239 N6-(pyridoxal phosphate)lysine.
{ECO:0000255|HAMAP-Rule:MF_01642}.
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


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