DAPAT_METJA
ID DAPAT_METJA Reviewed; 418 AA.
AC Q58786;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000303|PubMed:20418392};
DE Short=DAP-AT {ECO:0000303|PubMed:20418392};
DE Short=DAP-aminotransferase {ECO:0000303|PubMed:20418392};
DE Short=LL-DAP-aminotransferase {ECO:0000303|PubMed:20418392};
DE EC=2.6.1.83 {ECO:0000269|PubMed:20418392};
GN Name=dapL; OrderedLocusNames=MJ1391;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A DIAMINOPIMELATE AMINOTRANSFERASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=20418392; DOI=10.1128/jb.00172-10;
RA Liu Y., White R.H., Whitman W.B.;
RT "Methanococci use the diaminopimelate aminotransferase (DapL) pathway for
RT lysine biosynthesis.";
RL J. Bacteriol. 192:3304-3310(2010).
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, a reaction that requires three enzymes in E.coli.
CC {ECO:0000269|PubMed:20418392}.
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;
CC Evidence={ECO:0000269|PubMed:20418392};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20418392};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.42 uM for alpha-ketoglutarate (alpha-KG)(at pH 8.8 and at 70
CC degrees Celsius) {ECO:0000269|PubMed:20418392};
CC KM=82.8 uM for LL-2,6-diaminopimelate (L,L-DAP)(at pH 8.8 and at 70
CC degrees Celsius) {ECO:0000269|PubMed:20418392};
CC Vmax=0.39 umol/min/mg enzyme (at pH 8.8 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:20418392};
CC pH dependence:
CC Optimum pH is 8.5. About 40% and 50% of the maximum activity are
CC observed at pH 7.0 and 10.0, respectively.
CC {ECO:0000269|PubMed:20418392};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. No activity is detected at
CC temperatures below 45 degrees Celsius. At 85 degrees Celsius, the
CC activity is 85% of the maximum activity.
CC {ECO:0000269|PubMed:20418392};
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:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O84395}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L77117; AAB99401.1; -; Genomic_DNA.
DR PIR; F64473; F64473.
DR RefSeq; WP_010870908.1; NC_000909.1.
DR AlphaFoldDB; Q58786; -.
DR SMR; Q58786; -.
DR STRING; 243232.MJ_1391; -.
DR EnsemblBacteria; AAB99401; AAB99401; MJ_1391.
DR GeneID; 1452294; -.
DR KEGG; mja:MJ_1391; -.
DR eggNOG; arCOG01133; Archaea.
DR HOGENOM; CLU_017584_4_5_2; -.
DR InParanoid; Q58786; -.
DR OMA; YPHMPTG; -.
DR OrthoDB; 32104at2157; -.
DR PhylomeDB; Q58786; -.
DR BioCyc; MetaCyc:MON-15639; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; ISS:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
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 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..418
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000123929"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 115..116
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 140
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 190
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 221
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 248..250
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 259
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT MOD_RES 251
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O84395"
SQ SEQUENCE 418 AA; 47709 MW; 73CFBC48B4CA23F6 CRC64;
MESYIQNLFA ERIGGKKFGK EDVIYKFEKI KRAKQEAMKR HPDMELIDMG VGEPDEMADP
EVIRVLCEEA KKWENRGYAD NGIQELKDAV PPYMEKVYGV KDIDPVNEVI HSIGSKPALA
YITSAFINPG DVCLMTVPGY PVTATHTKWY GGEVYNLPLL EENDFLPDLE SIPEDIKKRA
KILYLNYPNN PTGAQATKKF YKEVVDFAFE NEVIVVQDAA YGALVYDGKP LSFLSVKDAK
EVGVEIHSFS KAFNMTGWRL AFLVGNELII KAFATVKDNF DSGQFIPIQK AGIYCLQHPE
ITERVRQKYE RRLRKMVKIL NEVGFKARMP GGTFYLYVKS PTKANGIEFK TAEDFSQYLI
KEKLISTVPW DDAGHYLRLA ACFVAKDENG NPTTEEKYED MVLEEFKRRL EGMDLEFE
