ID   MFNA_METKA              Reviewed;         372 AA.
AC   Q8TV92;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=MK1500;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02713.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TV92; -.
DR   SMR; Q8TV92; -.
DR   STRING; 190192.MK1500; -.
DR   EnsemblBacteria; AAM02713; AAM02713; MK1500.
DR   KEGG; mka:MK1500; -.
DR   PATRIC; fig|190192.8.peg.1658; -.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   UniPathway; UPA00080; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001826; 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   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; Reference proteome.
FT   CHAIN           1..372
FT                   /note="Probable L-tyrosine/L-aspartate decarboxylase"
FT                   /id="PRO_0000147024"
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   372 AA;  40407 MW;  FCB8BAE154F92E17 CRC64;
     MILQRDSDYS DGTVLGSMCT EPHPVAAEAF VAGLHVNLGD PYLFPNAYRA ERECIGWLAE
     TLLDHPAPEE AEGSIVSGGT EANILAAYAA REVTGGREII VPATRHFSFE KAARMLRMKL
     VEAPLRSDYT VDVDAVQDLI SRDTALIVGI VGTTETGSVD DIEALSDVAE DHGVPLHVDA
     AFGGFTAPFL REEYPLPRFG FDLEAVVSVT VDPHKMGLVP PPAGGIVFRD DEFPKAIEVY
     APYLSGGGAS QYTITGTRPG APVLALYANI LELGEEGYRR IAFRCYEETL KVAEKARELG
     LELAVDPPHL NLVNIRLPDR GTAERLLRES EREGWKISVS TKPLGVRIVM MPHLDAETVS
     RFLELVARVL GG