LYSJ_THEKO
ID LYSJ_THEKO Reviewed; 362 AA.
AC Q5JFW3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative [LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase {ECO:0000255|HAMAP-Rule:MF_02084};
DE EC=2.6.1.- {ECO:0000255|HAMAP-Rule:MF_02084};
DE EC=2.6.1.118 {ECO:0000255|HAMAP-Rule:MF_02084};
GN Name=lysJ {ECO:0000255|HAMAP-Rule:MF_02084}; OrderedLocusNames=TK0275;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {ECO:0000255|HAMAP-Rule:MF_02084}.
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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [amino-group carrier protein]-C-terminal-
CC gamma-(L-ornithyl)-L-glutamate = [amino-group carrier protein]-C-
CC terminal-gamma-(L-glutamyl-5-semialdehyde)-L-glutamate + L-glutamate;
CC Xref=Rhea:RHEA:52672, Rhea:RHEA-COMP:13327, Rhea:RHEA-COMP:13328,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:136761,
CC ChEBI:CHEBI:136763; Evidence={ECO:0000255|HAMAP-Rule:MF_02084};
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 -!- 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}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02084}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02084}.
CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC activity, thus carrying out the corresponding step in lysine
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. LysJ subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02084}.
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DR EMBL; AP006878; BAD84464.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5JFW3; -.
DR SMR; Q5JFW3; -.
DR STRING; 69014.TK0275; -.
DR EnsemblBacteria; BAD84464; BAD84464; TK0275.
DR KEGG; tko:TK0275; -.
DR PATRIC; fig|69014.16.peg.274; -.
DR eggNOG; arCOG00914; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR InParanoid; Q5JFW3; -.
DR OMA; PFMVPTY; -.
DR PhylomeDB; Q5JFW3; -.
DR UniPathway; UPA00033; UER00038.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..362
FT /note="Putative [LysW]-aminoadipate semialdehyde/glutamate
FT semialdehyde transaminase"
FT /id="PRO_0000112829"
FT BINDING 90..91
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 117
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 202..205
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
SQ SEQUENCE 362 AA; 40170 MW; 0165413621B3AC06 CRC64;
MPLYRKRLRL VRGEGVYVWD EKGRRYLDLI AGIGVNVLGH AHPEWVLDMS RQLEKIVVAG
PMFEHDEREE MLEELSHWVD YEYVYMGNSG TEAVEAAIKF ARLATGRSEI VAMTNAFHGR
TLGSLSATWK KKYREGFGPL VPGFKHIPFN NVEAAKEAIT KETAAVIFEP IQGEGGIVPA
DEEFVKTLRD LTEDVGALLI ADEVQSGLRT GKFLAIEHYG VRPDIVTMGK GIGNGFPVSL
TLTDLEIPRG KHGSTFGGNP LACRAVATTL RILRRDRLVE KAGEKFMEFS GERVVKTRGR
GLMIGIVLRR PAGNYVKALQ ERGILVNTAG NRVIRLLPPL IIEGDTLEEA RKEIEGVLND
IL
