LYSN_THET2
ID LYSN_THET2 Reviewed; 397 AA.
AC Q72LL6;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=2-aminoadipate transaminase;
DE EC=2.6.1.39;
DE AltName: Full=2-aminoadipate aminotransferase;
DE AltName: Full=Alpha-aminoadipate aminotransferase;
DE Short=AAA-AT;
DE Short=AadAT;
GN Name=lysN; OrderedLocusNames=TT_C0043;
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND NOMENCLATURE.
RX PubMed=15256574; DOI=10.1099/mic.0.27037-0;
RA Miyazaki T., Miyazaki J., Yamane H., Nishiyama M.;
RT "alpha-Aminoadipate aminotransferase from an extremely thermophilic
RT bacterium, Thermus thermophilus.";
RL Microbiology 150:2327-2334(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
RP MUTAGENESIS OF SER-20 AND ARG-23, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19632206; DOI=10.1016/j.bbrc.2009.07.096;
RA Ouchi T., Tomita T., Miyagawa T., Kuzuyama T., Nishiyama M.;
RT "Dual roles of a conserved pair, Arg23 and Ser20, in recognition of
RT multiple substrates in alpha-aminoadipate aminotransferase from Thermus
RT thermophilus.";
RL Biochem. Biophys. Res. Commun. 388:21-27(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RX PubMed=18831049; DOI=10.1002/prot.22245;
RA Tomita T., Miyagawa T., Miyazaki T., Fushinobu S., Kuzuyama T.,
RA Nishiyama M.;
RT "Mechanism for multiple-substrates recognition of alpha-aminoadipate
RT aminotransferase from Thermus thermophilus.";
RL Proteins 75:348-359(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
RA Tomita T., Miyazaki T., Miyagawa T., Fushinobu S., Kuzuyama T.,
RA Nishiyama M.;
RT "Crystal structure of lysN, alpha-aminoadipate aminotransferase, from
RT Thermus thermophilus HB27.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the transfer of an amino group between 2-oxoadipate
CC (2-OA) and glutamate (Glu) to yield alpha-aminodipate (AAA). It can
CC also transaminate glutamate, leucine, and aromatic amino acids. It also
CC contributes in the biosynthesis of other amino acids such as leucine.
CC {ECO:0000269|PubMed:15256574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-
CC glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39;
CC Evidence={ECO:0000269|PubMed:15256574};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.3 uM for 2-oxoisovalerate (at 45 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=24.2 uM for 2-oxoadipate (at 45 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=28.8 uM for 2-oxoisocaproate (at 45 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=148.3 uM for 2-oxo-3-methylvalerate (at 45 degrees Celsius and pH
CC 7.5) {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=300 uM for 2-oxoglutarate (at 45 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=460 uM for glutamate (at 45 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=810 uM for alpha-aminodipate (at 45 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=950 uM for leucine (at 45 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15256574, ECO:0000269|PubMed:19632206};
CC KM=381 mM for aspartate (with 1 mM of 2-oxoglutarate at 45 degrees
CC Celsius and pH 8.0) {ECO:0000269|PubMed:15256574,
CC ECO:0000269|PubMed:19632206};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 5/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15256574,
CC ECO:0000269|PubMed:18831049, ECO:0000269|PubMed:19632206,
CC ECO:0000269|Ref.5}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE017221; AAS80391.1; -; Genomic_DNA.
DR RefSeq; WP_011172501.1; NC_005835.1.
DR PDB; 2EGY; X-ray; 2.67 A; A/B/C/D=1-397.
DR PDB; 2Z1Y; X-ray; 1.75 A; A/B=1-397.
DR PDB; 2ZP7; X-ray; 2.26 A; A/B/C/D/E/F=1-397.
DR PDB; 2ZYJ; X-ray; 1.67 A; A/B=1-397.
DR PDB; 3CBF; X-ray; 1.67 A; A/B=1-397.
DR PDBsum; 2EGY; -.
DR PDBsum; 2Z1Y; -.
DR PDBsum; 2ZP7; -.
DR PDBsum; 2ZYJ; -.
DR PDBsum; 3CBF; -.
DR AlphaFoldDB; Q72LL6; -.
DR SMR; Q72LL6; -.
DR STRING; 262724.TT_C0043; -.
DR EnsemblBacteria; AAS80391; AAS80391; TT_C0043.
DR KEGG; tth:TT_C0043; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_6_0; -.
DR OMA; MRLNFTY; -.
DR OrthoDB; 1024978at2; -.
DR BRENDA; 2.6.1.39; 2305.
DR UniPathway; UPA00033; UER00031.
DR EvolutionaryTrace; Q72LL6; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..397
FT /note="2-aminoadipate transaminase"
FT /id="PRO_0000389636"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18831049,
FT ECO:0000269|PubMed:19632206"
FT BINDING 70
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 100..101
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 174
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18831049,
FT ECO:0000269|PubMed:19632206"
FT BINDING 202..205
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 235..237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 245
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18831049,
FT ECO:0000269|PubMed:19632206"
FT SITE 23
FT /note="Recognizes the side-chain carboxyl group of acidic
FT compounds"
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 20
FT /note="S->E: Strongly decreases the affinity for AAA and
FT Glu. A mild decrease of affinity is observed for 2-
FT oxoglutarate. Increases the affinity for leucine and 2-
FT oxoisocaproate."
FT /evidence="ECO:0000269|PubMed:19632206"
FT MUTAGEN 23
FT /note="R->A: Strongly decreases the affinity for AAA and
FT Glu. A mild decrease of affinity is observed for 2-
FT oxoglutarate which has the same chain length as Glu, but
FT differs by the presence of a 2-oxo group which is not
FT recognized by R-23. Increases the affinity for leucine and
FT 2-oxoisocaproate due to the absence of gamma-carboxyl
FT group."
FT /evidence="ECO:0000269|PubMed:19632206"
FT MUTAGEN 23
FT /note="R->Q: Strongly decreases the affinity for AAA and
FT Glu. A mild decrease of affinity is observed for 2-
FT oxoglutarate which has the same chain length as Glu, but
FT differs by the presence of a 2-oxo group which is not
FT recognized by R-23. Increases the affinity for leucine and
FT 2-oxoisocaproate due to the absence of gamma-carboxyl
FT group."
FT /evidence="ECO:0000269|PubMed:19632206"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2Z1Y"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 286..311
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:2ZYJ"
FT HELIX 376..396
FT /evidence="ECO:0007829|PDB:2ZYJ"
SQ SEQUENCE 397 AA; 43845 MW; A40FEA8E91D0AFDD CRC64;
MKPLSWSEAF GKGAGRIQAS TIRELLKLTQ RPGILSFAGG LPAPELFPKE EAAEAAARIL
REKGEVALQY SPTEGYAPLR AFVAEWIGVR PEEVLITTGS QQALDLVGKV FLDEGSPVLL
EAPSYMGAIQ AFRLQGPRFL TVPAGEEGPD LDALEEVLKR ERPRFLYLIP SFQNPTGGLT
PLPARKRLLQ MVMERGLVVV EDDAYRELYF GEARLPSLFE LAREAGYPGV IYLGSFSKVL
SPGLRVAFAV AHPEALQKLV QAKQGADLHT PMLNQMLVHE LLKEGFSERL ERVRRVYREK
AQAMLHALDR EVPKEVRYTR PKGGMFVWME LPKGLSAEGL FRRALEENVA FVPGGPFFAN
GGGENTLRLS YATLDREGIA EGVRRLGRAL KGLLALV
