TALY_CERS4
ID TALY_CERS4 Reviewed; 523 AA.
AC Q3IWB0;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tyrosine ammonia-lyase;
DE EC=4.3.1.23;
GN Name=hutH; ORFNames=RSP_3574;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF WILD-TYPE AND MUTANT PHE-89 IN
RP COMPLEXES WITH CINNAMAT; P-COUMARATE AND CAFFEATE, CATALYTIC ACTIVITY,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DEHYDRATION AT SER-150, AND
RP SUBUNIT.
RX PubMed=17185228; DOI=10.1016/j.chembiol.2006.11.011;
RA Louie G.V., Bowman M.E., Moffitt M.C., Baiga T.J., Moore B.S., Noel J.P.;
RT "Structural determinants and modulation of substrate specificity in
RT phenylalanine-tyrosine ammonia-lyases.";
RL Chem. Biol. 13:1327-1338(2006).
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-tyrosine. Has
CC very low phenylalanine ammonia-lyase activity (in vitro).
CC {ECO:0000269|PubMed:17185228}.
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:17185228};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=74.2 uM for L-Tyr {ECO:0000269|PubMed:17185228};
CC KM=11400 uM for L-Phe {ECO:0000269|PubMed:17185228};
CC Note=kcat is 4.32 sec(-1) for L-Tyr. kcat is 13.1 sec(-1) for L-Phe.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17185228}.
CC -!- INTERACTION:
CC Q3IWB0; Q3IWB0: hutH; NbExp=2; IntAct=EBI-9544445, EBI-9544445;
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.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; CP000144; ABA81174.1; -; Genomic_DNA.
DR RefSeq; WP_011339422.1; NZ_CP030272.1.
DR RefSeq; YP_355075.1; NC_007494.2.
DR PDB; 2O6Y; X-ray; 1.50 A; A/B/C/D/E/F/G/H=1-523.
DR PDB; 2O78; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-523.
DR PDB; 2O7B; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-523.
DR PDB; 2O7D; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-523.
DR PDB; 2O7E; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-523.
DR PDB; 2O7F; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-523.
DR PDBsum; 2O6Y; -.
DR PDBsum; 2O78; -.
DR PDBsum; 2O7B; -.
DR PDBsum; 2O7D; -.
DR PDBsum; 2O7E; -.
DR PDBsum; 2O7F; -.
DR AlphaFoldDB; Q3IWB0; -.
DR SMR; Q3IWB0; -.
DR STRING; 272943.RSP_3574; -.
DR DrugBank; DB01880; 3,4-Dihydroxycinnamic Acid.
DR DrugBank; DB04066; p-Coumaric acid.
DR EnsemblBacteria; ABA81174; ABA81174; RSP_3574.
DR KEGG; rsp:RSP_3574; -.
DR PATRIC; fig|272943.9.peg.4010; -.
DR eggNOG; COG2986; Bacteria.
DR OMA; MYVHSIP; -.
DR PhylomeDB; Q3IWB0; -.
DR BRENDA; 4.3.1.23; 5383.
DR SABIO-RK; Q3IWB0; -.
DR EvolutionaryTrace; Q3IWB0; -.
DR Proteomes; UP000002703; Chromosome 2.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0052883; F:tyrosine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0006572; P:tyrosine catabolic process; IDA:UniProtKB.
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 PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Phenylpropanoid metabolism; Reference proteome.
FT CHAIN 1..523
FT /note="Tyrosine ammonia-lyase"
FT /id="PRO_0000429968"
FT ACT_SITE 60
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT BINDING 303
FT /ligand="substrate"
FT BINDING 432..436
FT /ligand="substrate"
FT MOD_RES 150
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000305|PubMed:17185228"
FT CROSSLNK 149..151
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000305|PubMed:17185228"
FT MUTAGEN 89
FT /note="H->F: Abolishes tyrosine ammonia-lyase activity.
FT Increases affinity for L-Phe. Increases the low intrinsic
FT phenylalanine ammonia-lyase activity about twentyfold."
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:2O6Y"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2O7E"
FT HELIX 206..236
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:2O6Y"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 305..327
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 353..380
FT /evidence="ECO:0007829|PDB:2O6Y"
FT TURN 383..388
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:2O6Y"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 405..419
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2O6Y"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 442..475
FT /evidence="ECO:0007829|PDB:2O6Y"
FT TURN 476..481
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 484..494
FT /evidence="ECO:0007829|PDB:2O6Y"
FT HELIX 507..517
FT /evidence="ECO:0007829|PDB:2O6Y"
SQ SEQUENCE 523 AA; 54914 MW; ED77FA23DB0540B9 CRC64;
MLAMSPPKPA VELDRHIDLD QAHAVASGGA RIVLAPPARD RCRASEARLG AVIREARHVY
GLTTGFGPLA NRLISGENVR TLQANLVHHL ASGVGPVLDW TTARAMVLAR LVSIAQGASG
ASEGTIARLI DLLNSELAPA VPSRGTVGAS GDLTPLAHMV LCLQGRGDFL DRDGTRLDGA
EGLRRGRLQP LDLSHRDALA LVNGTSAMTG IALVNAHACR HLGNWAVALT ALLAECLRGR
TEAWAAALSD LRPHPGQKDA AARLRARVDG SARVVRHVIA ERRLDAGDIG TEPEAGQDAY
SLRCAPQVLG AGFDTLAWHD RVLTIELNAV TDNPVFPPDG SVPALHGGNF MGQHVALTSD
ALATAVTVLA GLAERQIARL TDERLNRGLP PFLHRGPAGL NSGFMGAQVT ATALLAEMRA
TGPASIHSIS TNAANQDVVS LGTIAARLCR EKIDRWAEIL AILALCLAQA AELRCGSGLD
GVSPAGKKLV QALREQFPPL ETDRPLGQEI AALATHLLQQ SPV
