ID R6N8H5_9FIRM Unreviewed; 393 AA.
AC R6N8H5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000256|ARBA:ARBA00018052, ECO:0000256|HAMAP-Rule:MF_01642};
DE Short=DAP-AT {ECO:0000256|HAMAP-Rule:MF_01642};
DE Short=DAP-aminotransferase {ECO:0000256|HAMAP-Rule:MF_01642};
DE Short=LL-DAP-aminotransferase {ECO:0000256|HAMAP-Rule:MF_01642};
DE EC=2.6.1.83 {ECO:0000256|ARBA:ARBA00013138, ECO:0000256|HAMAP-Rule:MF_01642};
GN Name=dapL {ECO:0000256|HAMAP-Rule:MF_01642};
GN ORFNames=BN531_01715 {ECO:0000313|EMBL:CDC02566.1};
OS Eubacterium sp. CAG:202.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262884 {ECO:0000313|EMBL:CDC02566.1, ECO:0000313|Proteomes:UP000017996};
RN [1] {ECO:0000313|EMBL:CDC02566.1, ECO:0000313|Proteomes:UP000017996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:202 {ECO:0000313|Proteomes:UP000017996};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate =
CC (S)-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:0000256|ARBA:ARBA00001493, ECO:0000256|HAMAP-
CC Rule:MF_01642};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|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:0000256|ARBA:ARBA00004982,
CC ECO:0000256|HAMAP-Rule:MF_01642}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01642}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01642}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDC02566.1}.
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; CBEO010000117; CDC02566.1; -; Genomic_DNA.
DR AlphaFoldDB; R6N8H5; -.
DR STRING; 1262884.BN531_01715; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000017996; Unassembled WGS sequence.
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 CDD; cd00609; AAT_like; 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.
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 PANTHER; PTHR43144:SF1; LL-DIAMINOPIMELATE AMINOTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01642,
KW ECO:0000313|EMBL:CDC02566.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01642};
KW Reference proteome {ECO:0000313|Proteomes:UP000017996};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01642, ECO:0000313|EMBL:CDC02566.1}.
FT DOMAIN 33..387
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 71
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 106..107
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 130
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 175
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 206
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 233..235
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 244
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 274
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
SQ SEQUENCE 393 AA; 43843 MW; B61609ED96153435 CRC64;
MQINRNFDNL VPNYLFAEVA SRTNKYMQEH PDKKVIKLGI GDVTLPLAPV VIEAMKKGAE
DLAHKDTFKG YPDYEGYAFL REAISNYYAG FGVTVDANEI FVSDGAKSDC GNIGDIFGKD
NVVLVTDPVY PVYVDSNIMA GRKIVYANSN RENNFAALPD ENVKADIIYL CSPNNPTGSA
YTADELKQWV DYAIKNDAII LYDAAYEAFI TEDLPRSIFA IEGARKCAIE MCSLSKTAGF
TGTRCGYTII PRELERDGHN IYNTWYRRQA TKFNGVSWPV QCAAAAVFSE EGQKQIKENI
SYYQDNARII SSAMDELGIY YTGGKNSPYI WLKCPNDMGS WEFFDLLLNE ANVVGTPGEG
FGKNGAGYFR LTSFGDRENT IEAVERIKKL LSK
//
