ID G2FYZ9_9FIRM Unreviewed; 390 AA.
AC G2FYZ9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=LL-diaminopimelate aminotransferase {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|HAMAP-Rule:MF_01642};
GN Name=dapL {ECO:0000256|HAMAP-Rule:MF_01642};
GN ORFNames=DOT_4965 {ECO:0000313|EMBL:EGW37153.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW37153.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW37153.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW37153.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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, ECO:0000256|RuleBase:RU000481};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EGW37153.1}.
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DR EMBL; AGAF01000231; EGW37153.1; -; Genomic_DNA.
DR RefSeq; WP_009623577.1; NZ_AGAF01000231.1.
DR AlphaFoldDB; G2FYZ9; -.
DR PATRIC; fig|913865.3.peg.4570; -.
DR eggNOG; COG0436; Bacteria.
DR OrthoDB; 9803354at2; -.
DR UniPathway; UPA00034; UER00466.
DR Proteomes; UP000004928; 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; IPR019881; DAP-NH2Trfase_DapL_Desulfo.
DR InterPro; IPR019942; DapL/ALD1.
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 NCBIfam; TIGR03540; DapC_direct; 1.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01642,
KW ECO:0000256|RuleBase:RU000481};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01642};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01642}.
FT DOMAIN 31..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 67
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 126
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 235..237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 246
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
SQ SEQUENCE 390 AA; 43309 MW; AF48FB35E5C21B14 CRC64;
MEEARRIQAL PPYLFARIDE KIAEAKAKGV DVISLGIGDP DLPTPDHIID KLVKAARNPV
NHRYPSYAGM LEFRQAVAEW YKRRSNIVID PQKEVVSLIG SKEGIAHIAF CYLNPGDIAL
IPDPGYPVYG VGTALAGGVP YALPLKEENG FLPELDRIPE EIAHKAKLMF LNYPNNPTGA
IADESFYMKV IAFAKKYDII ICHDGPYSEI AFNGYKPLSF LEVPGAKDVG IEFHSMSKTY
NMTGWRIGWA AGNARVIEAL GRIKSNIDTG VFQAIQEAAI EGLLGNQDII GENRKIYQER
QDIVIEGLTA LGWTVESPKA TIYVWPRVPK GFTSASFCEL VLDKTGVVIT PGNSYGEYGE
GYFRISLTTN TKRLREALQR LQDNFGKFEF
//
