ID A0A0C2M2K1_9CYAN Unreviewed; 411 AA.
AC A0A0C2M2K1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=SD80_27895 {ECO:0000313|EMBL:KIJ81406.1};
OS Scytonema tolypothrichoides VB-61278.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ81406.1};
RN [1] {ECO:0000313|EMBL:KIJ81406.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ81406.1};
RA Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL Submitted (JAN-2015) 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:KIJ81406.1}.
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DR EMBL; JXCA01000014; KIJ81406.1; -; Genomic_DNA.
DR STRING; 1233231.SD80_27895; -.
DR OrthoDB; 9802328at2; -.
DR UniPathway; UPA00034; UER00466.
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:KIJ81406.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01642};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01642, ECO:0000313|EMBL:KIJ81406.1}.
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 132
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 218
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 246..248
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 257
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 292
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01642"
SQ SEQUENCE 411 AA; 45184 MW; 2FDBDA5FAAA06570 CRC64;
MATINDNYLK LKAGYLFPEI ARRVNAFAQA NPDAKIIKLG IGDVTEPLPE ACRTAMIKAV
EEMGDRASFK GYGPEQGYTW LLEKIAAQDF QARGCEIDAL EIFVSDGSKC DTGNILDIFG
NDNIIAVTDP VYPVYVDTNV MAGHTGPAND KGEFEGLVYL PITAENNFTA EIPSQKVDLI
YLCFPNNPTG AVATKEHLKA WVDYARANGS IIFFDAAYEA YITDAELPHS IYEIEGAREC
AIEFRSFSKN AGFTGTRCAF TVVPKNLTAK AADGSDVELW KLWNRRQSTK FNGVSYIVQR
GAEAVYSQEG QAQIKELISF YLENAKIIRE KLTAAGLAVY GGVNAPYVWV QTPNGLSSWD
FFDKLLHTCN VVGTPGSGFG AAGEGYFRIS AFNSRENVEE AMKRITDRFT S
//
