ORNAT_THEKO
ID ORNAT_THEKO Reviewed; 445 AA.
AC Q5JEW1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ornithine aminotransferase {ECO:0000303|PubMed:29352105};
DE Short=Orn-AT {ECO:0000303|PubMed:29352105};
DE EC=2.6.1.13 {ECO:0000269|PubMed:29352105};
DE AltName: Full=Lysine aminotransferase {ECO:0000305};
DE Short=Lys-AT {ECO:0000303|PubMed:29352105};
DE EC=2.6.1.36 {ECO:0000269|PubMed:29352105};
GN OrderedLocusNames=TK2101 {ECO:0000312|EMBL:BAD86290.1};
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=KU216;
RX PubMed=29352105; DOI=10.1074/jbc.ra117.001222;
RA Zheng R.C., Hachisuka S.I., Tomita H., Imanaka T., Zheng Y.G.,
RA Nishiyama M., Atomi H.;
RT "An ornithine omega-aminotransferase required for growth in the absence of
RT exogenous proline in the archaeon Thermococcus kodakarensis.";
RL J. Biol. Chem. 293:3625-3636(2018).
CC -!- FUNCTION: L-ornithine aminotransferase involved in L-proline
CC biosynthesis. Also shows high activity toward L-lysine. 2-oxoglutarate
CC is the best amino acceptor, but 2-oxoadipate also leads to moderate
CC activity. {ECO:0000269|PubMed:29352105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-
CC semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13;
CC Evidence={ECO:0000269|PubMed:29352105};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysine = (S)-2-amino-6-oxohexanoate + L-
CC glutamate; Xref=Rhea:RHEA:21200, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:32551, ChEBI:CHEBI:58321; EC=2.6.1.36;
CC Evidence={ECO:0000269|PubMed:29352105};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P22256};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.80 mM for L-ornithine (in the presence of 5 mM 2-oxoglutarate)
CC {ECO:0000269|PubMed:29352105};
CC KM=1.71 mM for L-lysine (in the presence of 5 mM 2-oxoglutarate)
CC {ECO:0000269|PubMed:29352105};
CC KM=3.38 mM for 2-oxoglutarate (in the presence of 5 mM L-ornithine)
CC {ECO:0000269|PubMed:29352105};
CC KM=23.9 mM for 2-oxoadipate (in the presence of 5 mM L-ornithine)
CC {ECO:0000269|PubMed:29352105};
CC Vmax=93.8 umol/min/mg enzyme with L-ornithine as substrate (in the
CC presence of 5 mM 2-oxoglutarate) {ECO:0000269|PubMed:29352105};
CC Vmax=104 umol/min/mg enzyme with L-lysine as substrate (in the
CC presence of 5 mM 2-oxoglutarate) {ECO:0000269|PubMed:29352105};
CC Vmax=116 umol/min/mg enzyme with 2-oxoglutarate as substrate (in the
CC presence of 5 mM L-ornithine) {ECO:0000269|PubMed:29352105};
CC Vmax=149 umol/min/mg enzyme with 2-oxoadipate (in the presence of 5
CC mM L-ornithine) {ECO:0000269|PubMed:29352105};
CC Note=kcat is 77.6 sec(-1) with L-ornithine as substrate. kcat is 86.4
CC sec(-1) with L-lysine as substrate. kcat is 95.8 sec(-1) with 2-
CC oxoglutarate as substrate. kcat is 124 sec(-1) with 2-oxoadipate as
CC substrate. {ECO:0000269|PubMed:29352105};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:29352105};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:29352105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000269|PubMed:29352105}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29352105}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant cannot grow at all in the
CC absence of L-proline. {ECO:0000269|PubMed:29352105}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AP006878; BAD86290.1; -; Genomic_DNA.
DR RefSeq; WP_011251051.1; NC_006624.1.
DR AlphaFoldDB; Q5JEW1; -.
DR SMR; Q5JEW1; -.
DR STRING; 69014.TK2101; -.
DR EnsemblBacteria; BAD86290; BAD86290; TK2101.
DR GeneID; 3233911; -.
DR KEGG; tko:TK2101; -.
DR PATRIC; fig|69014.16.peg.2056; -.
DR eggNOG; arCOG00915; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR InParanoid; Q5JEW1; -.
DR OMA; DVFPRFA; -.
DR OrthoDB; 20774at2157; -.
DR PhylomeDB; Q5JEW1; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0045484; F:L-lysine 6-transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
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 PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Proline biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="Ornithine aminotransferase"
FT /id="PRO_0000449043"
FT BINDING 124..125
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 320
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P22256"
SQ SEQUENCE 445 AA; 49675 MW; EA34B5936E137512 CRC64;
MVVRPNVKEL PGPKAKEVIE RNFKYLAMTT QDPENLPIVI ERGEGIRVYD VDGNVFYDFA
SGVGVINVGH SHPRVVEAIK KQAEKFTHYS LTDFFYENAI ILAEKLIELA PGDIERKVVY
GNSGAEANEA AMKLVKYGTG RKQFLAFYHA FHGRTQAVLS LTASKWVQQD GFFPTMPGVT
HIPYPNPYRN TWGIDGYEEP DELTNRVLDF IEEYVFRHVP PHEIGAIFFE PIQGEGGYVV
PPKGFFKALK KFADEYGILL ADDEVQMGIG RTGKFWAIEH FGVEPDLIQF GKAIGGGLPL
AGVIHRADIT FDKPGRHATT FGGNPVAIAA GIEVVEIVKE LLPHVQEVGD YLHKYLEEFK
EKYEVIGDAR GLGLAQAVEI VKSKETKEKY PELRDRIVKE SAKRGLVLLG CGDNSIRFIP
PLIVTKEEID VAMEIFEEAL KAALK
