DAPAT_PARUW
ID DAPAT_PARUW Reviewed; 411 AA.
AC Q6MDE0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:17093042};
DE Short=DAP-AT {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:17093042};
DE Short=DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:17093042};
DE Short=LL-DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000303|PubMed:17093042};
DE EC=2.6.1.83 {ECO:0000255|HAMAP-Rule:MF_01642, ECO:0000269|PubMed:17093042};
GN Name=dapL {ECO:0000255|HAMAP-Rule:MF_01642}; Synonyms=aspC;
GN OrderedLocusNames=pc0685;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=17093042; DOI=10.1073/pnas.0608643103;
RA McCoy A.J., Adams N.E., Hudson A.O., Gilvarg C., Leustek T., Maurelli A.T.;
RT "L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by
RT Chlamydia and plants for synthesis of diaminopimelate/lysine.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17909-17914(2006).
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 use meso-diaminopimelate, lysine or
CC ornithine as substrates. {ECO:0000269|PubMed:17093042}.
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:17093042};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01642,
CC ECO:0000269|PubMed:17093042};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for LL-2,6-diaminopimelate (at 30 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17093042};
CC KM=1.1 mM for 2-oxoglutarate (at 30 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17093042};
CC KM=5 uM for L-2,3,4,5-tetrahydrodipicolinate (at 30 degrees Celsius
CC and pH 7.6) {ECO:0000269|PubMed:17093042};
CC KM=0.4 mM for glutamic acid (at 30 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17093042};
CC Vmax=1.84 umol/min/mg enzyme for the forward reaction (at 30 degrees
CC Celsius and pH 7.6) {ECO:0000269|PubMed:17093042};
CC Vmax=0.09 umol/min/mg enzyme for the reverse reaction (at 30 degrees
CC Celsius and pH 7.6) {ECO:0000269|PubMed:17093042};
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 -!- SEQUENCE CAUTION:
CC Sequence=CAF23409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX908798; CAF23409.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044044859.1; NC_005861.1.
DR AlphaFoldDB; Q6MDE0; -.
DR SMR; Q6MDE0; -.
DR STRING; 264201.pc0685; -.
DR PRIDE; Q6MDE0; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_051433_0_0_0; -.
DR OMA; DFQARGC; -.
DR OrthoDB; 417859at2; -.
DR BRENDA; 2.6.1.83; 10176.
DR SABIO-RK; Q6MDE0; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000000529; 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..411
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000312005"
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 105..106
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 129
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 245..247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 287
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ SEQUENCE 411 AA; 45911 MW; 66F6EEF66F1B194F CRC64;
MVKRNVHLTK LQSGYLFPEI NRRKNEFLKK HPSAQLINLG IGDTTQPIPL YISEAMQNFA
KQLASEKTYR GYGTEQGSIL LREAIAEQYY QGKIDPQEVF VSDGSKCDVG RLQILFGSDA
TIAVQNPTYP AYVDTGVING QASFFQTSTK QYQRITYMSC LPENNFFPDL ANLPKTDLIY
FCSPNNPTGS AATNEQLREL VQFAKKRQSI IIFDAAYASF VRSSHIPRSI YEIEGAKEVA
IEVGSFSKMI GFTGVRLGWS VVPKQLRFED GHSVQQDWER IVCTFFNGAS NIAQAGGLAA
LQKEGLQAID ELSSYYMKNS NILKKAFEEC GYKVYGGENV PYLWVHFPQL TSWEAFEILL
KQSQLVSVPG SGFGSAGEGF LRFSAFGKQS DITVALPRIK HALLKIKPTV Y
