TAM_CHOCO
ID TAM_CHOCO Reviewed; 531 AA.
AC Q0VZ68;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Tyrosine 2,3-aminomutase {ECO:0000303|PubMed:19222035};
DE EC=5.4.3.6;
DE AltName: Full=Tyrosine ammonia-lyase {ECO:0000303|PubMed:19222035};
DE EC=4.3.1.23;
GN Name=cmdF {ECO:0000312|EMBL:CAJ46694.1};
OS Chondromyces crocatus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Chondromyces.
OX NCBI_TaxID=52;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ46694.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Cm c5 {ECO:0000312|EMBL:CAJ46694.1};
RX PubMed=16793524; DOI=10.1016/j.chembiol.2006.06.002;
RA Rachid S., Krug D., Kunze B., Kochems I., Scharfe M., Zabriskie T.M.,
RA Blocker H., Muller R.;
RT "Molecular and biochemical studies of chondramide formation-highly
RT cytotoxic natural products from Chondromyces crocatus Cm c5.";
RL Chem. Biol. 13:667-681(2006).
RN [2] {ECO:0000305}
RP FUNCTION.
RC STRAIN=Cm c5 {ECO:0000269|PubMed:17545150};
RX PubMed=17545150; DOI=10.1074/jbc.m703439200;
RA Rachid S., Krug D., Weissman K.J., Muller R.;
RT "Biosynthesis of (R)-beta-tyrosine and its incorporation into the highly
RT cytotoxic chondramides produced by Chondromyces crocatus.";
RL J. Biol. Chem. 282:21810-21817(2007).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PHE-57; 60-LEU--ILE-65; 79-ARG--ALA-83; GLY-184; LYS-242;
RP 275-VAL--GLY-288; PRO-377; 399-GLU--THR-406; GLU-399 AND 427-ASN--VAL-433.
RC STRAIN=Cm c5 {ECO:0000269|PubMed:19222035};
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 aminomutase and, to a lesser extent, ammonia-lyase
CC activity. Primarily, catalyzes the rearrangement of L-tyrosine to R-
CC beta-tyrosine, which is incorporated into secondary metabolites called
CC chondramides. The aminomutase activity mainly produces R-beta-tyrosine
CC but also S-beta tyrosine in smaller amounts. Does not accept D-
CC tyrosine, L-histidine or L-phenylalanine as substrates.
CC {ECO:0000269|PubMed:16793524, ECO:0000269|PubMed:17545150,
CC 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 -!- 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=377 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 -!- MISCELLANEOUS: Chondramides are secondary metabolites with antifungal
CC and cytotoxic activity. They are non-ribosomally produced depsipeptides
CC consisting of a polyketide chain and 3 amino acids (alanine, N-
CC methyltryptophan and beta-tyrosine or alpha-methoxy-beta-tyrosine).
CC -!- SIMILARITY: Belongs to the TAL/TAM family.
CC {ECO:0000269|PubMed:19222035}.
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DR EMBL; AM179409; CAJ46694.1; -; Genomic_DNA.
DR RefSeq; WP_050432503.1; NZ_CP012159.1.
DR AlphaFoldDB; Q0VZ68; -.
DR SMR; Q0VZ68; -.
DR STRING; 52.CMC5_047490; -.
DR OrthoDB; 715502at2; -.
DR BRENDA; 5.4.3.6; 11879.
DR SABIO-RK; Q0VZ68; -.
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 GO; GO:0009403; P:toxin biosynthetic 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 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.
FT CHAIN 1..531
FT /note="Tyrosine 2,3-aminomutase"
FT /id="PRO_0000407375"
FT ACT_SITE 51
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 141
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:P21310,
FT ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 140..142
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:P21310"
FT MUTAGEN 57
FT /note="F->Y: Loss of aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 60..65
FT /note="LVPVMI->MIYMLV: Shift towards ammonia lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 79..83
FT /note="RSHAA->YHLAT: Total loss of aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 79..82
FT /note="RSHA->TFLS: Total loss of aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 184
FT /note="G->R: Gain of aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 242
FT /note="K->R: Gain of aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 275..288
FT /note="Missing: Total loss of aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 377
FT /note="P->R: No effect."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 396
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 399..406
FT /note="EGGQYLAT->MIAQVTSA: Residual aminomutase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 399
FT /note="E->A: Loss of aminomutase activity and increased
FT product racemization. Gain of ammonia-lyase activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 399
FT /note="E->K: Loss of aminomutase and ammonia-lyase
FT activity. Higher enantiomeric excess of (R)-beta-tyrosine."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 399
FT /note="E->M: Loss of aminomutase and ammonia-lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 427..433
FT /note="NGSNQDV->SAGREDH: Total loss of aminomutase
FT activity."
FT /evidence="ECO:0000269|PubMed:19222035"
FT MUTAGEN 427..433
FT /note="NGSNQDV->SANQEDH: Total loss of aminomutase
FT activity."
FT /evidence="ECO:0000269|PubMed:19222035"
SQ SEQUENCE 531 AA; 56901 MW; 07A542D37EA339E0 CRC64;
MKITGSNLSI YDVADVCMKR ATVELDPSQL ERVAVAHERT QAWGEAQHPI YGVNTGFGEL
VPVMIPRQHK RELQENLIRS HAAGGGEPFA DDVVRAIMLA RLNCLMKGYS GASVETVKLL
AEFINRGIHP VIPQQGSLGA SGDLSPLSHI ALALIGEGTV SFKGQVRKTG DVLREEGLKP
LELGFKGGLT LINGTSAMTG AACVALGRAY HLFRLALLAT ADFVQCLGGS TGPFEERGHL
PKNHSGQVIV AREIRKLLAG SQLTSDHQDL MKEMVARSGV GNDVVDTGVY LQDAYTLRAV
PQILGPVLDT LDFARKLIEE ELNSTNDNPL IFDVPEQTFH GANFHGQYVA MACDYLNIAV
TEIGVLAERQ LNRLVDPNIN GKLPPFLASA HSGLLCGFEG GQYLATSIAS ENLDLAAPSS
IKSLPSNGSN QDVVSMGTTS ARKSLRLCEN VGTIVSTLIA ACNQAGHILG NERFSPPIRE
LHGELSRSVP LYQDDSPIFE LFQTVRAFVG GDGFRAHLVT HLDLAATTAS S
