ID   MFNA_METM5              Reviewed;         384 AA.
AC   A4G060;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=MmarC5_1547;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO35844.1; -; Genomic_DNA.
DR   RefSeq; WP_011869291.1; NC_009135.1.
DR   AlphaFoldDB; A4G060; -.
DR   SMR; A4G060; -.
DR   STRING; 402880.MmarC5_1547; -.
DR   EnsemblBacteria; ABO35844; ABO35844; MmarC5_1547.
DR   GeneID; 4929048; -.
DR   KEGG; mmq:MmarC5_1547; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   OrthoDB; 44488at2157; -.
DR   UniPathway; UPA00080; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000253; 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; 3.40.640.10; -; 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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..384
FT                   /note="Probable L-tyrosine/L-aspartate decarboxylase"
FT                   /id="PRO_1000069444"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   384 AA;  43335 MW;  975070E3893365A2 CRC64;
     MEEQDILNEL RKYRSQDLKY EEGYILGSMC TKPHPIARKI SEMFFETNLG DPGLFNGTSK
     LEKEVVSMLG SILHNNNAFG YIISGGTEAN LTAMRAFKNI SKSKDKKQNI IIPETAHFSF
     DKARDMMDLN VVRPPLTEYF TMDVKFIRDY VEDSKNEISG IVGIAGCTEL GSIDNIYELS
     KIAVENDILL HVDAAFGGFV IPFLDDKYKL KGYNYDFDFS LNGVSSITID PHKMGLAPIS
     AGGILFRDNT FKKYLDVDAP YLTEKQQATL IGTRSGVGVA STWGIMKLLG IEGYENLVNE
     SMEKTKHLVK KAREYGFETA IDPVMNIVAL KDENKQDTCM KLREENWYVS VCRCVEALRI
     VVMPHLEIEH IDGFLESLSN TKKY