ID DAPAT_CROS5 Reviewed; 411 AA. AC B1WSG7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 02-SEP-2026, entry version 88. 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}; GN OrderedLocusNames=cce_2605; OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain OS ATCC 51142)). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica. OX NCBI_TaxID=43989; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51142 / BH68; RX PubMed=18812508; DOI=10.1073/pnas.0805418105; RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.; RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium RT important in the marine nitrogen cycle."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(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. {ECO:0000255|HAMAP-Rule:MF_01642}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,6S)-2,6-diaminopimelate + 2-oxoglutarate = (S)-2,3,4,5- CC tetrahydrodipicolinate + L-glutamate + H2O + H(+); 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}. 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; CP000806; ACB51953.1; -; Genomic_DNA. DR RefSeq; WP_009544705.1; NC_010546.1. DR AlphaFoldDB; B1WSG7; -. DR SMR; B1WSG7; -. DR STRING; 43989.cce_2605; -. DR KEGG; cyt:cce_2605; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_051433_0_0_3; -. DR OrthoDB; 9802328at2; -. DR UniPathway; UPA00034; UER00466. DR Proteomes; UP000001203; Chromosome circular. DR GO; GO:0010285; F:L,L-diaminopimelate:2-oxoglutarate transaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR CDD; cd00609; AAT_like; 1. DR FunFam; 3.40.640.10:FF:000099; LL-diaminopimelate aminotransferase, chloroplastic; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_01642; DapL_aminotrans_1; 1. DR InterPro; IPR004839; Aminotransferase_I/II_large. 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 NCBIfam; TIGR03542; DAPAT_plant; 1. DR PANTHER; PTHR43144; AMINOTRANSFERASE; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..411 FT /note="LL-diaminopimelate aminotransferase" FT /id="PRO_1000186860" 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 187 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 218 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 246..248 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 257 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 292 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 292 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT BINDING 388 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" FT MOD_RES 249 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642" SQ SEQUENCE 411 AA; 45374 MW; 97CAC8BC8F6A582C CRC64; MATINDNYLK LKAGYLFPEI ARRVNTFIEA NPEAKIIKLG IGDVTEPLPE ACRTAMIKAV EDMGDRSSFK GYGPEQGYGW LREKIAAQDF QARGCDIDAS EIFVSDGAKC DTGNILDIFG KNNKIAVTDP VYPVYVDTNV MAGHTGETNE KGEYEGLVYL PISADNHFVA DIPSEKVDLI YLCFPNNPTG ATATKEYLKA WVDYATANDS IIFFDAAYEA FITDESLPHS IYEIEGAKDC AIEFRSFSKN AGFTGTRCAF TVVPKQLTAK ASDGSQVELW KLWNRRQSTK FNGVSYIVQR GAEAVYSEAG KAQIKGLVSF YLENAKIICE QLKSAGFEVY GGVNAPYIWL KTPHNLSSWD FFDKLLQTTH VVGTPGSGFG AAGEGYFRIS AFNSRENVEE AMKRITQAFK V //