ID   MFNA_METAR              Reviewed;         375 AA.
AC   Q0W498;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Probable L-tyrosine/L-aspartate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01610};
DE            Short=TDC/ADC {ECO:0000255|HAMAP-Rule:MF_01610};
DE            EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01610};
DE            EC=4.1.1.25 {ECO:0000255|HAMAP-Rule:MF_01610};
GN   Name=mfnA {ECO:0000255|HAMAP-Rule:MF_01610};
GN   OrderedLocusNames=UNCMA_14340; ORFNames=RCIX1543;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
CC   -!- FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce
CC       tyramine for methanofuran biosynthesis. Can also catalyze the
CC       decarboxylation of L-aspartate to produce beta-alanine for coenzyme A
CC       (CoA) biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01610}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315,
CC         ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01610};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01610};
CC   -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01610}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01610}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. MfnA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01610}.
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DR   EMBL; AM114193; CAJ36795.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0W498; -.
DR   SMR; Q0W498; -.
DR   STRING; 351160.RCIX1543; -.
DR   KEGG; rci:RCIX1543; -.
DR   PATRIC; fig|351160.9.peg.1479; -.
DR   eggNOG; arCOG00027; Archaea.
DR   OrthoDB; 56891at2157; -.
DR   UniPathway; UPA00080; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000663; Chromosome.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001120; P:methanofuran biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01610; MfnA_decarbox; 1.
DR   InterPro; IPR020931; MfnA.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03812; tyr_de_CO2_Arch; 1.
DR   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Probable L-tyrosine/L-aspartate decarboxylase"
FT                   /id="PRO_0000293191"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   375 AA;  41138 MW;  E8990460A4847961 CRC64;
     MRERGLGEEE IFAELCEARS RDVPYGRVLS SMCTNPHPIA VKAHQEFVNT NLGDPKLFPG
     TADIEHRCIG LIGDLLHLPA ATGYISTGGT ESNIQALRTA IQMKHTDRRR ANIVVPESAH
     YSFEKASQML GIAIRRAPLD DLLRADPSEM AALIDKNTIA LVAVAGTTEF GQIDPIEEIG
     RLAQEHDLYL HVDAAFGGFV IPFMDRPAKF DFEIPGVQSI TIDPHKMGLS TIPSGGLLYR
     SESLMKVLEI NAQYLTSMVQ TSLAGTRSGA SAASAYAVLQ YLGRAGYREI VATCMENTRI
     LREQLEDMGM EPIIEPVLNI VTARAKDPVG LRKKLAEKNW YVSTTVHPCA LRMVVMPHVT
     ADVIEAFTAD LKKVI
//