MFNA_METAC
ID MFNA_METAC Reviewed; 395 AA.
AC Q8TUQ9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=MA_0006;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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; AE010299; AAM03460.1; -; Genomic_DNA.
DR RefSeq; WP_011020065.1; NC_003552.1.
DR AlphaFoldDB; Q8TUQ9; -.
DR SMR; Q8TUQ9; -.
DR STRING; 188937.MA_0006; -.
DR EnsemblBacteria; AAM03460; AAM03460; MA_0006.
DR GeneID; 1471898; -.
DR KEGG; mac:MA_0006; -.
DR HOGENOM; CLU_028929_2_1_2; -.
DR InParanoid; Q8TUQ9; -.
DR OMA; DPHKMGL; -.
DR OrthoDB; 44488at2157; -.
DR PhylomeDB; Q8TUQ9; -.
DR UniPathway; UPA00080; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..395
FT /note="Probable L-tyrosine/L-aspartate decarboxylase"
FT /id="PRO_0000147022"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ SEQUENCE 395 AA; 43305 MW; C412ABC0DA58ED03 CRC64;
MNEQGLSEKE IFSYLENAKS EDTDYYRVLS SMCTHPHKIA VEANRLFIEA NLGDLGLFAG
ASRLEQEVVG MLGELLHAPS IDVPFGGSCE SSACGYLTTG GTESNIQAVR GMKNLVTTGK
KELKGAPNIV IPESAHFSFD KVADMMGIEV RRASLDSEFR VDMASIESLI DANTIGLIGI
AGNTEFGQID PIDKLSEIAL ENELFLHIDA AFGGFVIPFL EKPQPFDFKL PGVTSIAVDP
HKMGLSTIPS GALLFRSASF LDSLKVNTPY LTTKAQFTLT GTRSGASAAA TCAVMKYLGN
EGYRKNVQYC MQLTEKLVIE ARKIGFEPLL EPVMNVVALK VPNPDFVREQ MLERFGWNVS
ITRTPRALRL VLMPHNTLED IEIFVQDLKE VTVEI
