TALY_CUPMC
ID TALY_CUPMC Reviewed; 533 AA.
AC Q1LRV9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Tyrosine ammonia-lyase {ECO:0000303|PubMed:19222035};
DE Short=CmTAL {ECO:0000303|PubMed:19222035};
DE EC=4.3.1.23;
DE AltName: Full=Tyrosine 2,3-aminomutase {ECO:0000303|PubMed:19222035};
DE EC=5.4.3.6;
GN OrderedLocusNames=Rmet_0231;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19222035; DOI=10.1002/cbic.200800748;
RA Krug D., Muller R.;
RT "Discovery of additional members of the tyrosine aminomutase enzyme family
RT and the mutational analysis of CmdF.";
RL ChemBioChem 10:741-750(2009).
CC -!- FUNCTION: Has ammonia-lyase and, to a lesser extent, aminomutase
CC activity. Catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine
CC and S-beta-tyrosine. Does not accept L-histidine or L-phenylalanine as
CC substrates. {ECO:0000269|PubMed:19222035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine = (E)-4-coumarate + NH4(+); Xref=Rhea:RHEA:24906,
CC ChEBI:CHEBI:12876, ChEBI:CHEBI:28938, ChEBI:CHEBI:58315; EC=4.3.1.23;
CC Evidence={ECO:0000269|PubMed:19222035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate;
CC Xref=Rhea:RHEA:15781, ChEBI:CHEBI:57956, ChEBI:CHEBI:58315;
CC EC=5.4.3.6; Evidence={ECO:0000269|PubMed:19222035};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=348 uM for L-tyrosine (tyrosine 2,3-aminomutase activity)
CC {ECO:0000269|PubMed:19222035};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000250}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000250|UniProtKB:P21310}.
CC -!- SIMILARITY: Belongs to the TAL/TAM family.
CC {ECO:0000269|PubMed:19222035}.
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DR EMBL; CP000352; ABF07117.1; -; Genomic_DNA.
DR RefSeq; WP_011515131.1; NC_007973.1.
DR AlphaFoldDB; Q1LRV9; -.
DR SMR; Q1LRV9; -.
DR STRING; 266264.Rmet_0231; -.
DR EnsemblBacteria; ABF07117; ABF07117; Rmet_0231.
DR KEGG; rme:Rmet_0231; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_1_4; -.
DR OMA; MYVHSIP; -.
DR OrthoDB; 715502at2; -.
DR SABIO-RK; Q1LRV9; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0016841; F:ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0050368; F:tyrosine 2,3-aminomutase activity; IDA:UniProtKB.
DR GO; GO:0052883; F:tyrosine ammonia-lyase activity; IEA:UniProtKB-EC.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR InterPro; IPR022314; Tyr_aminomutase.
DR PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR03832; Tyr_2_3_mutase; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Lyase; Reference proteome.
FT CHAIN 1..533
FT /note="Tyrosine ammonia-lyase"
FT /id="PRO_0000407374"
FT ACT_SITE 57
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:P21310,
FT ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 146..148
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:P21310"
SQ SEQUENCE 533 AA; 56163 MW; 37618DC17B19CC44 CRC64;
MPHAHPADID GHHLTPDTVA AIARGQRAAI VPEPVLGKVA DARARFEQVA AANVPIYGVS
TGFGELVHNW VDIEHGRALQ ENLLRSHCAG VGPLFSRDEV RAMMVARANA LARGYSAVRP
AVIEQLLKYL EAGITPAVPQ VGSLGASGDL APLSHVAITL IGEGKVLTED GGTAPTAEVL
RERGITPLAL AYKEGLALIN GTSAMTGVSC LLLETLRAQV QQAEIIAALA LEGLSASADA
FMAHGHDIAK PHPGQIRSAA NMRALLADSA RLSGHGELSA EMKTRAGEAK NTGTGVFIQK
AYTLRCIPQV LGAVRDTLDH CATVVERELN SSNDNPLFFE DGELFHGGNF HGQQVAFAMD
FLAIAATQLG VVSERRLNRL LSPHLNNNLP AFLAAANEGL SCGFAGAQYP ATALIAENRT
ICSPASIQSV PSNGDNQDVV SMGLIAARNA RRILDNNQYI LALELLASCQ AAELAGAVEQ
LAPAGRAVFA FVRERVPFLS IDRYMTDDIE AMAALLRQGA LVEVVRGAGI ELA
