ID   MFNA_METBF              Reviewed;         395 AA.
AC   Q46DU3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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}; OrderedLocusNames=Mbar_A0977;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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; CP000099; AAZ69949.1; -; Genomic_DNA.
DR   RefSeq; WP_011305998.1; NC_007355.1.
DR   AlphaFoldDB; Q46DU3; -.
DR   SMR; Q46DU3; -.
DR   STRING; 269797.Mbar_A0977; -.
DR   EnsemblBacteria; AAZ69949; AAZ69949; Mbar_A0977.
DR   GeneID; 3625749; -.
DR   KEGG; mba:Mbar_A0977; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   OrthoDB; 44488at2157; -.
DR   UniPathway; UPA00080; -.
DR   UniPathway; UPA00241; -.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..395
FT                   /note="Probable L-tyrosine/L-aspartate decarboxylase"
FT                   /id="PRO_0000293187"
FT   MOD_RES         242
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   395 AA;  43889 MW;  0F96E6DDD3EB2D71 CRC64;
     MNEQGLSEKE IFSYLEDVKS EDTDYYRVLS SMCTHPHRIA VEAHRLFIEA NLGDLGLFAG
     AHRLEKEVIR MLGELLHAQS VEIPSGEACE SSVCGYLTTG GTESNIQAIR GMKNLVTEDG
     KKSGEILNIV VPESAHFSFD KVANMMGIEV KRASLDPEFR VDIASAESLI DANTIGLVGI
     AGNTEFGQVD PIEELSKLAL ENELFLHVDA AFGGFVIPFL EKPYSFDFKV PGVTSIAIDP
     HKMGLSTIPS GALLFRSPFF MDSLKVNTPY LTTKSQFTLT GTRSGASAAA TYAVMKYLGR
     EGYRKNVQYC MQLTTKLVKE ARKFGFEPLI EPVMNVVDLR VPNPDIVREQ LLKKFGWNVS
     ITRNPRSLRL VLMPHNTARD IEEFLQDLRK VTTEL