ID LYSJ_THET2 Reviewed; 395 AA. AC Q93R93; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-SEP-2026, entry version 153. DE RecName: Full=[LysW]-aminoadipate semialdehyde transaminase {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305}; DE EC=2.6.1.118 {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|PubMed:19620981}; GN Name=lysJ {ECO:0000255|HAMAP-Rule:MF_02084, GN ECO:0000303|PubMed:11489859}; OrderedLocusNames=TT_C1393; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RP PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=11489859; DOI=10.1128/jb.183.17.5067-5073.2001; RA Miyazaki J., Kobashi N., Nishiyama M., Yamane H.; RT "Functional and evolutionary relationship between arginine biosynthesis and RT prokaryotic lysine biosynthesis through alpha-aminoadipate."; RL J. Bacteriol. 183:5067-5073(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=19620981; DOI=10.1038/nchembio.198; RA Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T., RA Nishiyama C., Kuzuyama T., Nishiyama M.; RT "Discovery of proteinaceous N-modification in lysine biosynthesis of RT Thermus thermophilus."; RL Nat. Chem. Biol. 5:673-679(2009). CC -!- FUNCTION: Catalyzes the transfer of the amino group of L-glutamate to CC [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine CC (Probable). In vitro, can use N(2)-acetyl-L-ornithine and N(2)-acetyl- CC L-lysine (PubMed:11489859). {ECO:0000269|PubMed:11489859, CC ECO:0000305|PubMed:19620981}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L- CC glutamate + 2-oxoglutarate = [amino-group carrier protein]-C- CC terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate; CC Xref=Rhea:RHEA:41952, Rhea:RHEA-COMP:9714, Rhea:RHEA-COMP:9715, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:78501, CC ChEBI:CHEBI:78526; EC=2.6.1.118; Evidence={ECO:0000255|HAMAP- CC Rule:MF_02084, ECO:0000305|PubMed:19620981}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02084}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_02084}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.8 mM for N(2)-acetyl-L-ornithine {ECO:0000269|PubMed:11489859}; CC KM=10 mM for N(2)-acetyl-L-lysine {ECO:0000269|PubMed:11489859}; CC Note=kcat is 1.0 sec(-1) with N(2)-acetyl-L-ornithine as substrate. CC kcat is 0.8 sec(-1) with N(2)-acetyl-L-lysine as substrate. CC {ECO:0000269|PubMed:11489859}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5. CC {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000269|PubMed:11489859, CC ECO:0000269|PubMed:19620981}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02084, CC ECO:0000269|PubMed:11489859}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02084}. CC -!- DISRUPTION PHENOTYPE: Auxotroph for lysine. CC {ECO:0000269|PubMed:11489859}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. LysJ subfamily. {ECO:0000255|HAMAP- CC Rule:MF_02084, ECO:0000305}. CC -!- CAUTION: Was originally thought (PubMed:11489859) to be an N(2)-acetyl- CC L-2-aminoadipate semialdehyde transaminase. {ECO:0000305}. 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; AB055203; BAB61775.1; -; Genomic_DNA. DR EMBL; AE017221; AAS81735.1; -; Genomic_DNA. DR RefSeq; WP_011173776.1; NC_005835.1. DR AlphaFoldDB; Q93R93; -. DR SMR; Q93R93; -. DR KEGG; tth:TT_C1393; -. DR eggNOG; COG4992; Bacteria. DR HOGENOM; CLU_016922_10_0_0; -. DR OrthoDB; 29163at2; -. DR BioCyc; MetaCyc:MONOMER-6741; -. DR BRENDA; 2.6.1.118; 2305. DR UniPathway; UPA00033; UER00038. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 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_02084; LysJ_aminotrans_3; 1. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR050103; Class-III_PLP-dep_AT. DR InterPro; IPR053513; Class-III_PLP_Aminotransferase. DR InterPro; IPR037537; LysJ. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR00707; argD; 1. DR NCBIfam; NF042418; LysJ_Th_th; 1. DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Lysine biosynthesis; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..395 FT /note="[LysW]-aminoadipate semialdehyde transaminase" FT /id="PRO_0000112806" FT BINDING 113..114 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" FT BINDING 140 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" FT BINDING 225..228 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" FT BINDING 282 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" FT BINDING 283 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" FT MOD_RES 254 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084" SQ SEQUENCE 395 AA; 43451 MW; 1D29F8E7585A5C3A CRC64; METRTLEDWR ALLEAEKTLD SGVYNKHDLL IVRGQGARVW DAEGNEYIDC VGGYGVANLG HGNPEVVEAV KRQAETLMAM PQTLPTPMRG EFYRTLTAIL PPELNRVFPV NSGTEANEAA LKFARAHTGR KKFVAAMRGF SGRTMGSLSV TWEPKYREPF LPLVEPVEFI PYNDVEALKR AVDEETAAVI LEPVQGEGGV RPATPEFLRA AREITQEKGA LLILDEIQTG MGRTGKRFAF EHFGIVPDIL TLAKALGGGV PLGVAVMREE VARSMPKGGH GTTFGGNPLA MAAGVAAIRY LERTRLWERA AELGPWFMEK LRAIPSPKIR EVRGMGLMVG LELKEKAAPY IARLEKEHRV LALQAGPTVI RFLPPLVIEK EDLERVVEAV RAVLA //