LYSJ_THET8
ID LYSJ_THET8 Reviewed; 395 AA.
AC Q5SHH5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=[LysW]-aminoadipate semialdehyde transaminase {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=TTHA1755;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS
RP AND PLP.
RG RIKEN structural genomics initiative (RSGI);
RT "Three-dimensional structure of acetylornithine aminotransferase from
RT Thermus thermophilus HB8.";
RL Submitted (AUG-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the transfer of the amino group of L-glutamate to
CC [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine.
CC {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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02084}.
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; AP008226; BAD71578.1; -; Genomic_DNA.
DR RefSeq; WP_011228893.1; NC_006461.1.
DR RefSeq; YP_145021.1; NC_006461.1.
DR PDB; 1VEF; X-ray; 1.35 A; A/B=1-395.
DR PDB; 1WKG; X-ray; 2.25 A; A/B=1-395.
DR PDB; 1WKH; X-ray; 2.25 A; A/B=1-395.
DR PDBsum; 1VEF; -.
DR PDBsum; 1WKG; -.
DR PDBsum; 1WKH; -.
DR AlphaFoldDB; Q5SHH5; -.
DR SMR; Q5SHH5; -.
DR STRING; 300852.55773137; -.
DR EnsemblBacteria; BAD71578; BAD71578; BAD71578.
DR GeneID; 3169449; -.
DR KEGG; ttj:TTHA1755; -.
DR PATRIC; fig|300852.9.peg.1726; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_0; -.
DR OMA; GMTTQIY; -.
DR PhylomeDB; Q5SHH5; -.
DR UniPathway; UPA00033; UER00038.
DR EvolutionaryTrace; Q5SHH5; -.
DR Proteomes; UP000000532; 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 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Lysine biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="[LysW]-aminoadipate semialdehyde transaminase"
FT /id="PRO_0000311262"
FT BINDING 113..114
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000269|Ref.2"
FT BINDING 140
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000305|Ref.2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000305|Ref.2"
FT BINDING 225..228
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000305|Ref.2"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000305|Ref.2"
FT BINDING 283
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000269|Ref.2"
FT MOD_RES 254
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084,
FT ECO:0000269|Ref.2"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 113..128
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1VEF"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1VEF"
FT TURN 227..234
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 288..304
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 307..322
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1VEF"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:1VEF"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:1VEF"
SQ SEQUENCE 395 AA; 43423 MW; 1D3B73EAC3454C3A 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 PLGAAVMREE VARSMPKGGH GTTFGGNPLA MAAGVAAIRY
LERTRLWERA AELGPWFMEK LRAIPSPKIR EVRGMGLMVG LELKEKAAPY IARLEKEHRV
LALQAGPTVI RFLPPLVIEK EDLERVVEAV RAVLA
