ID   TAM_MYXFU               Reviewed;         526 AA.
AC   B8ZV93;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Tyrosine 2,3-aminomutase {ECO:0000303|PubMed:19222035};
DE            Short=MfTAM {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=tam {ECO:0000312|EMBL:CAR79033.1};
OS   Myxococcus fulvus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=33;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAR79033.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Mx f65 {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 much lesser extent, ammonia-lyase
CC       activity. Primarily, catalyzes the rearrangement of L-tyrosine to S-
CC       beta-tyrosine, which is probably incorporated into secondary metabolite
CC       myxovalargin. The aminomutase activity exclusively produces S-beta-
CC       tyrosine. {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   -!- 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; FM212243; CAR79033.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8ZV93; -.
DR   SMR; B8ZV93; -.
DR   BRENDA; 5.4.3.6; 11880.
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   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   Isomerase; Lyase.
FT   CHAIN           1..526
FT                   /note="Tyrosine 2,3-aminomutase"
FT                   /id="PRO_0000407376"
FT   ACT_SITE        41
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         131
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250|UniProtKB:P21310,
FT                   ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        130..132
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:P21310"
SQ   SEQUENCE   526 AA;  56959 MW;  15DD2AA7BF124099 CRC64;
     MDIYAVAVGR VGVELDAAQL ERVRATHLRV QGWGMEKYPM YGVNTGFGEL INVIIPPQFK
     SDLQHNLLRS HAAGGGEPFP DEVVRAIMTV RINCLMKGYS GISPEALQLL ATMLNRGIHP
     VIPMQGSLGA SGDLAPLSHM ALPLIGDGHV RKNGVTRPTM EVFQEEGLTP LKLGFKEGLA
     LVNGTSAMTG AASLALYRAR HLLRLSLLAS ADIVQAMNAS TRPFSHTGNA LKNHPGQVVI
     ARLMRDLTQG TGLMRDHQDI MRAISERTSH SNDVEETEIY LQNAYSLRCM PQVLGVVLET
     LQMCQRFIEE EANSVNDNPV ILDTPAETYH GANFHGQYVA MACDYLSIAV AEMGVLAERQ
     LNRLLDPHIN KPLPGFLAHA KTGLFCGFEG GQYLATSIAS ENLDLAAPSS IKSIPSNGQN
     QDIVSMGLIA ARKTLALCEN VGTILSVLMA ALNQASHFTE AAKYSAPIRS IHEKLGKVAP
     RYEDERPMST VIAQVRGVLL QEQGLALAQS LVNLDLTPDL SLEPRA