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DAPAT_ACET2
ID   DAPAT_ACET2             Reviewed;         410 AA.
AC   A3DK17;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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};
GN   Name=dapL {ECO:0000255|HAMAP-Rule:MF_01642}; OrderedLocusNames=Cthe_3101;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION AS A LL-DAP AMINOTRANSFERASE, SUBSTRATE 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. Can also use m-DAP instead of LL-DAP as the amino-
CC       group donor. {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};
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       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; CP000568; ABN54296.1; -; Genomic_DNA.
DR   RefSeq; WP_003511604.1; NC_009012.1.
DR   AlphaFoldDB; A3DK17; -.
DR   SMR; A3DK17; -.
DR   STRING; 203119.Cthe_3101; -.
DR   EnsemblBacteria; ABN54296; ABN54296; Cthe_3101.
DR   KEGG; cth:Cthe_3101; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_051433_0_0_9; -.
DR   OMA; DFQARGC; -.
DR   OrthoDB; 417859at2; -.
DR   UniPathway; UPA00034; UER00466.
DR   Proteomes; UP000002145; 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; Reference proteome; Transferase.
FT   CHAIN           1..410
FT                   /note="LL-diaminopimelate aminotransferase"
FT                   /id="PRO_0000342227"
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   410 AA;  46283 MW;  08837998422DA39E CRC64;
     MAFINENYLK LPGSYLFSEI ARRVDNFRKE NPNAKIIRLG IGDVTKPLAP AVIDALHKAV
     DEMAKEETFK GYGPEQGYSF LVSKIIEYDY MPRGIRLDED EVFVSDGAKS DTGNFQEIFG
     LDNKVAVTDP VYPVYVDSNV MAGRTGKYLA NGYFENITYL PCTAENNFIP ELPKEKVDII
     YLCFPNNPTG MTLSREELKK WVDYARENRA IILFDSAYEA YIREKDVPHS IYEVEGADEV
     AIEFRSFSKT AGFTGTRCAY TVVPKKVVAY TKNGEAHQLN SLWNRRQTTK FNGVPYIIQR
     AAAAVYTPEG QKQTKETIDY YMENAKIIKQ GLEDIGLTVF GGVNAPYIWL KTPDGISSWE
     FFDIMLKEIN VVGTPGSGFG PSGEGYFRLT AFGSRENTLE AVERFKNLKF
 
 
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