ID R5BJA8_9FIRM Unreviewed; 140 AA.
AC R5BJA8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000256|ARBA:ARBA00018052};
DE EC=2.6.1.83 {ECO:0000256|ARBA:ARBA00013138};
GN ORFNames=BN814_02371 {ECO:0000313|EMBL:CCX55508.1};
OS Veillonella sp. CAG:933.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1262980 {ECO:0000313|EMBL:CCX55508.1, ECO:0000313|Proteomes:UP000018347};
RN [1] {ECO:0000313|EMBL:CCX55508.1, ECO:0000313|Proteomes:UP000018347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:933 {ECO:0000313|Proteomes:UP000018347};
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 -!- 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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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 -!- 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:CCX55508.1}.
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DR EMBL; CAWP010000119; CCX55508.1; -; Genomic_DNA.
DR AlphaFoldDB; R5BJA8; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000018347; Unassembled WGS sequence.
DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR019942; DapL/ALD1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:CCX55508.1};
KW Transferase {ECO:0000313|EMBL:CCX55508.1}.
FT DOMAIN 25..135
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 140 AA; 15643 MW; 287FA33D41465A37 CRC64;
MADGQKQALN PMWNRRQCTK FNGVPYIIQR AAEAVYSEAG HRQTREAIAY YKENARIIRE
GLTAIGLTVF GGVDAPYIWL KVPAGMTSWE FFDLLLGKVH IVSTPGAGFG PCGEGYLRLT
SFGSRENTLR AIERIKTLQF
//