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TPL_CLOTE
ID   TPL_CLOTE               Reviewed;         460 AA.
AC   Q897C2;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tyrosine phenol-lyase {ECO:0000255|HAMAP-Rule:MF_00543};
DE            EC=4.1.99.2 {ECO:0000255|HAMAP-Rule:MF_00543};
DE   AltName: Full=Beta-tyrosinase {ECO:0000255|HAMAP-Rule:MF_00543};
GN   Name=tpl {ECO:0000255|HAMAP-Rule:MF_00543}; OrderedLocusNames=CTC_00818;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tyrosine = NH4(+) + phenol + pyruvate;
CC         Xref=Rhea:RHEA:21704, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15882, ChEBI:CHEBI:28938, ChEBI:CHEBI:58315; EC=4.1.99.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00543};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00543};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00543}.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00543}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO35416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015927; AAO35416.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035110530.1; NC_004557.1.
DR   AlphaFoldDB; Q897C2; -.
DR   SMR; Q897C2; -.
DR   STRING; 212717.CTC_00818; -.
DR   PRIDE; Q897C2; -.
DR   EnsemblBacteria; AAO35416; AAO35416; CTC_00818.
DR   GeneID; 64181064; -.
DR   KEGG; ctc:CTC_00818; -.
DR   HOGENOM; CLU_047223_0_0_9; -.
DR   OMA; VYTYAHM; -.
DR   OrthoDB; 91973at2; -.
DR   Proteomes; UP000001412; Chromosome.
DR   GO; GO:0050371; F:tyrosine phenol-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006570; P:tyrosine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00543; Tyr_phenol_lyase; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR011166; Beta-eliminating_lyase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR018176; Tryptophanase_CS.
DR   InterPro; IPR013441; Tyr_phenol_ly.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF001386; Trpase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02618; tyr_phenol_ly; 1.
DR   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..460
FT                   /note="Tyrosine phenol-lyase"
FT                   /id="PRO_0000195632"
FT   MOD_RES         260
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00543"
SQ   SEQUENCE   460 AA;  51760 MW;  57F19258AD7813C1 CRC64;
     MDLSKYPAEP FKIKSVEPVK MISREEREIA MKEAGYNTFN LRSEDVYIDL LTDSGTNAMS
     DAQWAGMMIG DEAYAGSKNW LFLESTIKEL FGFKHVVPTH QGRGAENLLS SIAIKPGQYV
     AGNMYFTTTR YHQEKNGGIF VDIIRDEAHD ASIDIPFKGN IDVNKLEKLI EEKGAENIAY
     VCLAVTVNLA GGQPVSMANM RAVRELTAKH GIKVFYDATR CVENAYFIKE QEEGYADVSI
     KDIVHEMFSY SDGATMSGKK DGIVNIGGFL AINDEELFGK AKEIVVVYEG MPSYGGMTGR
     DMQAIAIGFR EAMQYEYIEH RIRQVRYLGD RLKEAGVPIV EPVGGHAVFL DARRFCPHLD
     QEQFPAQSLA ASLYIDSGVR SMERGIVSAG RDVNTGENHK PKLETVRLTI PRRVYTYKHM
     DVVAESVIHL YKHKEDIRPL KFTYEPAQLR FFTAKFDYAD
 
 
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