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Tyrosine 2,3-aminomutase (EC 5.4.3.6) (Tyrosine ammonia-lyase) (EC 4.3.1.23)

 TAM_CHOCO               Reviewed;         531 AA.
Q0VZ68;
03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
31-JAN-2018, entry version 55.
RecName: Full=Tyrosine 2,3-aminomutase {ECO:0000303|PubMed:19222035};
EC=5.4.3.6;
AltName: Full=Tyrosine ammonia-lyase {ECO:0000303|PubMed:19222035};
EC=4.3.1.23;
Name=cmdF {ECO:0000312|EMBL:CAJ46694.1};
Chondromyces crocatus.
Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
Sorangiineae; Polyangiaceae; Chondromyces.
NCBI_TaxID=52;
[1] {ECO:0000305, ECO:0000312|EMBL:CAJ46694.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=Cm c5 {ECO:0000312|EMBL:CAJ46694.1};
PubMed=16793524; DOI=10.1016/j.chembiol.2006.06.002;
Rachid S., Krug D., Kunze B., Kochems I., Scharfe M., Zabriskie T.M.,
Blocker H., Muller R.;
"Molecular and biochemical studies of chondramide formation-highly
cytotoxic natural products from Chondromyces crocatus Cm c5.";
Chem. Biol. 13:667-681(2006).
[2] {ECO:0000305}
FUNCTION.
STRAIN=Cm c5 {ECO:0000269|PubMed:17545150};
PubMed=17545150; DOI=10.1074/jbc.M703439200;
Rachid S., Krug D., Weissman K.J., Muller R.;
"Biosynthesis of (R)-beta-tyrosine and its incorporation into the
highly cytotoxic chondramides produced by Chondromyces crocatus.";
J. Biol. Chem. 282:21810-21817(2007).
[3] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF PHE-57; 60-LEU--ILE-65; 79-ARG--ALA-83; GLY-184;
LYS-242; 275-VAL--GLY-288; PRO-377; 399-GLU--THR-406; GLU-399 AND
427-ASN--VAL-433.
STRAIN=Cm c5 {ECO:0000269|PubMed:19222035};
PubMed=19222035; DOI=10.1002/cbic.200800748;
Krug D., Muller R.;
"Discovery of additional members of the tyrosine aminomutase enzyme
family and the mutational analysis of CmdF.";
ChemBioChem 10:741-750(2009).
-!- FUNCTION: Has aminomutase and, to a lesser extent, ammonia-lyase
activity. Primarily, catalyzes the rearrangement of L-tyrosine to
R-beta-tyrosine, which is incorporated into secondary metabolites
called chondramides. The aminomutase activity mainly produces R-
beta-tyrosine but also S-beta tyrosine in smaller amounts. Does
not accept D-tyrosine, L-histidine or L-phenylalanine as
substrates. {ECO:0000269|PubMed:16793524,
ECO:0000269|PubMed:17545150, ECO:0000269|PubMed:19222035}.
-!- CATALYTIC ACTIVITY: L-tyrosine = 3-amino-3-(4-
hydroxyphenyl)propanoate. {ECO:0000269|PubMed:19222035}.
-!- CATALYTIC ACTIVITY: L-tyrosine = trans-p-hydroxycinnamate +
ammonia. {ECO:0000269|PubMed:19222035}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=377 uM for L-tyrosine (tyrosine 2,3-aminomutase activity)
{ECO:0000269|PubMed:19222035};
-!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000250}.
-!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO),
which is formed autocatalytically by cyclization and dehydration
of residues Ala-Ser-Gly. {ECO:0000250|UniProtKB:P21310}.
-!- MISCELLANEOUS: Chondramides are secondary metabolites with
antifungal and cytotoxic activity. They are non-ribosomally
produced depsipeptides consisting of a polyketide chain and 3
amino acids (alanine, N-methyltryptophan and beta-tyrosine or
alpha-methoxy-beta-tyrosine).
-!- SIMILARITY: Belongs to the TAL/TAM family.
{ECO:0000269|PubMed:19222035}.
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EMBL; AM179409; CAJ46694.1; -; Genomic_DNA.
RefSeq; WP_050432503.1; NZ_CP012159.1.
ProteinModelPortal; Q0VZ68; -.
SMR; Q0VZ68; -.
BRENDA; 5.4.3.6; 11879.
GO; GO:0016841; F:ammonia-lyase activity; IDA:UniProtKB.
GO; GO:0050368; F:tyrosine 2,3-aminomutase activity; IDA:UniProtKB.
GO; GO:0052883; F:tyrosine ammonia-lyase activity; IEA:UniProtKB-EC.
GO; GO:0009403; P:toxin biosynthetic process; IDA:UniProtKB.
CDD; cd00332; PAL-HAL; 1.
Gene3D; 1.10.275.10; -; 1.
InterPro; IPR001106; Aromatic_Lyase.
InterPro; IPR024083; Fumarase/histidase_N.
InterPro; IPR008948; L-Aspartase-like.
InterPro; IPR022313; Phe/His_NH3-lyase_AS.
InterPro; IPR022314; Tyr_aminomutase.
PANTHER; PTHR10362; PTHR10362; 1.
Pfam; PF00221; Lyase_aromatic; 1.
SUPFAM; SSF48557; SSF48557; 1.
TIGRFAMs; TIGR03832; Tyr_2_3_mutase; 1.
PROSITE; PS00488; PAL_HISTIDASE; 1.
1: Evidence at protein level;
Isomerase; Lyase.
CHAIN 1 531 Tyrosine 2,3-aminomutase.
/FTId=PRO_0000407375.
ACT_SITE 51 51 Proton donor/acceptor. {ECO:0000250}.
BINDING 81 81 Substrate. {ECO:0000250}.
BINDING 193 193 Substrate. {ECO:0000250}.
BINDING 298 298 Substrate. {ECO:0000250}.
MOD_RES 141 141 2,3-didehydroalanine (Ser).
{ECO:0000250|UniProtKB:P21310,
ECO:0000255|PROSITE-ProRule:PRU10122}.
CROSSLNK 140 142 5-imidazolinone (Ala-Gly).
{ECO:0000250|UniProtKB:P21310}.
MUTAGEN 57 57 F->Y: Loss of aminomutase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 60 65 LVPVMI->MIYMLV: Shift towards ammonia
lyase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 79 83 RSHAA->YHLAT: Total loss of aminomutase
activity. {ECO:0000269|PubMed:19222035}.
MUTAGEN 79 82 RSHA->TFLS: Total loss of aminomutase
activity. {ECO:0000269|PubMed:19222035}.
MUTAGEN 184 184 G->R: Gain of aminomutase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 242 242 K->R: Gain of aminomutase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 275 288 Missing: Total loss of aminomutase
activity. {ECO:0000269|PubMed:19222035}.
MUTAGEN 377 377 P->R: No effect.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 396 396 C->S: No effect.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 399 406 EGGQYLAT->MIAQVTSA: Residual aminomutase
activity. {ECO:0000269|PubMed:19222035}.
MUTAGEN 399 399 E->A: Loss of aminomutase activity and
increased product racemization. Gain of
ammonia-lyase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 399 399 E->K: Loss of aminomutase and ammonia-
lyase activity. Higher enantiomeric
excess of (R)-beta-tyrosine.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 399 399 E->M: Loss of aminomutase and ammonia-
lyase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 427 433 NGSNQDV->SAGREDH: Total loss of
aminomutase activity.
{ECO:0000269|PubMed:19222035}.
MUTAGEN 427 433 NGSNQDV->SANQEDH: Total loss of
aminomutase activity.
{ECO:0000269|PubMed:19222035}.
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


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