LYSJ_THET2
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 03-AUG-2022, entry version 136.
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, ECO:0000303|PubMed:11489859};
GN OrderedLocusNames=TT_C1393;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; 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=2-oxoglutarate + [amino-group carrier protein]-C-terminal-
CC gamma-(L-lysyl)-L-glutamate = [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}.
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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 STRING; 262724.TT_C1393; -.
DR EnsemblBacteria; AAS81735; AAS81735; TT_C1393.
DR KEGG; tth:TT_C1393; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_0; -.
DR OMA; GMTTQIY; -.
DR OrthoDB; 572533at2; -.
DR BioCyc; MetaCyc:MON-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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_02084; LysJ_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
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 Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00707; argD; 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; 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
