ID E1L6H1_9FIRM Unreviewed; 409 AA.
AC E1L6H1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000256|ARBA:ARBA00018052};
DE EC=2.6.1.83 {ECO:0000256|ARBA:ARBA00013138};
GN ORFNames=HMPREF9321_0497 {ECO:0000313|EMBL:EFL56058.1};
OS Veillonella atypica ACS-049-V-Sch6.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL56058.1, ECO:0000313|Proteomes:UP000004211};
RN [1] {ECO:0000313|EMBL:EFL56058.1, ECO:0000313|Proteomes:UP000004211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL56058.1,
RC ECO:0000313|Proteomes:UP000004211};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFL56058.1}.
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DR EMBL; AEDR01000029; EFL56058.1; -; Genomic_DNA.
DR RefSeq; WP_005377212.1; NZ_AEDR01000029.1.
DR AlphaFoldDB; E1L6H1; -.
DR eggNOG; COG0436; Bacteria.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000004211; 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 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:0000313|EMBL:EFL56058.1};
KW Transferase {ECO:0000313|EMBL:EFL56058.1}.
FT DOMAIN 35..404
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 409 AA; 45533 MW; 018F4099A9108509 CRC64;
MANINENYLN LQGSYLFANI AKKVADYQAA HPDADIIRLG IGDVTLPLVP AIVDAMTKAV
QEMGKAETFR GYGPEQGYDF LRKAIIEGDY KPYGIEISMD EVFVSDGAKS DVGNIQELFS
EDNIIAITDP VYPVYLDSNV MGGRTGQAVD GMFEKVVYLP TFAENNFSPE FPAERVDIVY
LCSPNNPTGT VLSRARLAEW IKWCKENDAI LMFDSAYEAF ISTEDTVKSI YEIEGAREVA
IEFRSFSKTA GFTGTRCAYA VVPKEVTGKT KSGERQPLNP MWNRRQCTKF NGVPYIVQRG
AEAVYSKEGR EQTRANIAYY KENARIIKEG LESIGLTVYG GTDAPYIWLK TPGNMTSWEL
FDLLLEKVQI VSTPGSGFGP HGEGYLRLTA FGSRENTIRA VERIKTLQF
//
