DAPAT_METMP
ID DAPAT_METMP Reviewed; 416 AA.
AC Q6LX26;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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:0000250|UniProtKB:Q58786};
GN Name=dapL; OrderedLocusNames=MMP1527;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP LACK OF FUNCTION AS A DIAMINOPIMELATE AMINOTRANSFERASE.
RX PubMed=18371309; DOI=10.1016/j.febslet.2008.03.021;
RA Graham D.E., Huse H.K.;
RT "Methanogens with pseudomurein use diaminopimelate aminotransferase in
RT lysine biosynthesis.";
RL FEBS Lett. 582:1369-1374(2008).
RN [3]
RP FUNCTION IN LYSINE BIOSYNTHESIS AND AS A DIAMINOPIMELATE AMINOTRANSFERASE,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=S2 / LL;
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. {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:0000250|UniProtKB:Q58786};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q58786};
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow in the
CC absence of exogenous L-lysine. {ECO:0000269|PubMed:20418392}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BX950229; CAF31083.1; -; Genomic_DNA.
DR RefSeq; WP_011171471.1; NC_005791.1.
DR AlphaFoldDB; Q6LX26; -.
DR SMR; Q6LX26; -.
DR STRING; 267377.MMP1527; -.
DR EnsemblBacteria; CAF31083; CAF31083; MMP1527.
DR GeneID; 41280164; -.
DR KEGG; mmp:MMP1527; -.
DR PATRIC; fig|267377.15.peg.1564; -.
DR eggNOG; arCOG01133; Archaea.
DR HOGENOM; CLU_017584_4_5_2; -.
DR OMA; YPHMPTG; -.
DR OrthoDB; 32104at2157; -.
DR BioCyc; MMAR267377:MMP_RS07845-MON; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000000590; 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; ISS:UniProtKB.
DR GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; IDA: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..416
FT /note="LL-diaminopimelate aminotransferase"
FT /id="PRO_0000342259"
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 416 AA; 46764 MW; 8D3A9D91C9275F0E CRC64;
MESYIQNLFA ERIGGKSFGK EDVIYKFEKI KRAKQAAKLK YPDMELIDMG VGEPDEMADE
SVVEVLCEEA KKHVNRGYSD NGVQALKDEI PIYLEKIFGV KDLDPVNEVV HSIGSKPALA
YITSVFINPG DVTLMTVPGY PVTATHTKWY GGSVETLPLL EKNNFLPELD AISKEVRENA
KILYLNYPNN PTGAQATKKF YKEAVDFAFE NDLIVIQDAA YAALTYGDKP LSFLSVKDAK
EVGVEIHSFS KAYNMTGWRL AFVAGNELIV RGFAAVKDNY DSGQFIPIQK AGIHCLRHPE
ITEKTRAKYE RRLSKMVKIL KEAGFNAKMP GGTFYLYVKA PIGTKDGAKF ANAEEFSQFM
IKEKLISTVP WDDAGNFVRM AACFEAFKDG EISIEEEDRI LNEVKRRLTE VEFVFE
