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Database: UniProt
Entry: E3MC55_CAERE
LinkDB: E3MC55_CAERE
Original site: E3MC55_CAERE 
ID   E3MC55_CAERE            Unreviewed;       464 AA.
AC   E3MC55;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Tyrosine aminotransferase {ECO:0000256|ARBA:ARBA00015959, ECO:0000256|PIRNR:PIRNR000517};
DE            Short=TAT {ECO:0000256|PIRNR:PIRNR000517};
DE            EC=2.6.1.5 {ECO:0000256|ARBA:ARBA00012749, ECO:0000256|PIRNR:PIRNR000517};
GN   Name=Cre-tatn-1 {ECO:0000313|EMBL:EFO98254.1};
GN   ORFNames=CRE_15311 {ECO:0000313|EMBL:EFO98254.1}, FL81_03739
GN   {ECO:0000313|EMBL:POM50046.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFO98254.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|EMBL:EFO98254.1};
RG   The Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:POM50046.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM50046.1};
RX   PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA   Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA   Ahearne T.E., Cutter A.D., Phillips P.C.;
RT   "Reproductive Mode and the Evolution of Genome Size and Structure in
RT   Caenorhabditis Nematodes.";
RL   PLoS Genet. 11:e1005323-e1005323(2015).
RN   [4] {ECO:0000313|EMBL:POM50046.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM50046.1};
RX   PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA   Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA   Ahearne T.E., Cutter A.D., Phillips P.C.;
RT   "Correction: Reproductive Mode and the Evolution of Genome Size and
RT   Structure in Caenorhabditis Nematodes.";
RL   PLoS Genet. 11:e1005497-e1005497(2015).
RN   [5] {ECO:0000313|EMBL:POM50046.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM50046.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC       tyrosine to p-hydroxyphenylpyruvate. {ECO:0000256|PIRNR:PIRNR000517}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC         glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001125,
CC         ECO:0000256|PIRNR:PIRNR000517};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRNR:PIRNR000517, ECO:0000256|PIRSR:PIRSR000517-1};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC       {ECO:0000256|ARBA:ARBA00005203, ECO:0000256|PIRNR:PIRNR000517}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|PIRNR:PIRNR000517}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|PIRNR:PIRNR000517}.
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DR   EMBL; DS268434; EFO98254.1; -; Genomic_DNA.
DR   EMBL; LFJK02000005; POM50046.1; -; Genomic_DNA.
DR   RefSeq; XP_003106312.1; XM_003106264.1.
DR   AlphaFoldDB; E3MC55; -.
DR   STRING; 31234.E3MC55; -.
DR   EnsemblMetazoa; CRE15311.1; CRE15311.1; WBGene00058557.
DR   GeneID; 9807729; -.
DR   KEGG; crq:GCK72_025638; -.
DR   CTD; 9807729; -.
DR   eggNOG; KOG0259; Eukaryota.
DR   HOGENOM; CLU_017584_4_2_1; -.
DR   OMA; CALDLCI; -.
DR   OrthoDB; 5474881at2759; -.
DR   UniPathway; UPA00139; UER00338.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0043053; P:dauer entry; IEA:EnsemblMetazoa.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   InterPro; IPR005958; TyrNic_aminoTrfase.
DR   InterPro; IPR005957; Tyrosine_aminoTrfase.
DR   NCBIfam; TIGR01264; tyr_amTase_E; 1.
DR   NCBIfam; TIGR01265; tyr_nico_aTase; 1.
DR   PANTHER; PTHR45744; TYROSINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR45744:SF2; TYROSINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR000517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          74..434
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         284
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ   SEQUENCE   464 AA;  51110 MW;  EFFECD4F1758383B CRC64;
     MQTLMTHSRI NPLPGAITKE EIKCQLLVHE RRFLSKPAKK DEWNVMPQSV HSKNTVNPVR
     KIADACAVPP NPEKKVIRLH LGDPSVGGKL PPSEVAVQAM HESVSNHIYD GYGPAVGALA
     ARQAIVDKYS SIDNEFTADD VVLASGCSHA LQMAIEAVAN AGDNILVPHP GFPLYSTLCR
     PHNIIDKPYK IDMSGEDVKI DLSYMATIID DNTKAIIINN PGNPTGGVFT KEHLEEILEF
     ANKYKLIIIA DEIYGDLVYN GATFYPLASL SPKVPIITCD GIAKRWMVPG WRLGWLIIHN
     HFGVLTEVKK GIVALSQKIV GPCSLVQGAL PKILRETSEE YFVYTRNVIE TNANIVEDIL
     AEVPGMRVVK PKGAMYMMVN ISKTAYGSDV SFCQNLIKEE SVFCLPGQAF SAPGYFRVVL
     TSSTDDMEEA AMRIRDFCFR NFNQHSDSED SSDEGLDLSA MESD
//
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