ID MFNA_METVS Reviewed; 384 AA.
AC A6URB4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Mevan_1136;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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; CP000742; ABR55036.1; -; Genomic_DNA.
DR RefSeq; WP_012065951.1; NC_009634.1.
DR AlphaFoldDB; A6URB4; -.
DR SMR; A6URB4; -.
DR STRING; 406327.Mevan_1136; -.
DR GeneID; 5325833; -.
DR KEGG; mvn:Mevan_1136; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_028929_2_1_2; -.
DR OrthoDB; 56891at2157; -.
DR UniPathway; UPA00080; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001107; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
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_1000069446"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ SEQUENCE 384 AA; 43124 MW; 04D9E2448771E805 CRC64;
MDELSILNEL RKYRDMDLDY EDGTILGSMC TKPHPLTRKI SEMFFETNLG DPGLFKGTRE
LEKQAISMIG NVLGNKDAFG YIISGGTEAN LTAMRAFKNV SKKSGKSLNI IIPETAHFSF
DKAKDIMDLN VIRPPLTKYF TMDVKFIRDY VFDNPNKISG IVGISGCTEL GSIDNIAELS
KIAVDNDILL HVDAAFGGFV IPFLYDKYKL KNYRYEFDFS LEGVSSITID PHKMGLAPIS
AGGILFRNNS FKKYLDVDSP YLTEKQQATL IGTRSGVGAA ATWGVMKLLG TSGYKKIVND
SMEKTYYLTR KLREYGFKTA IDPVINIVSI VDEHKNETCA KLRENGFHVS VSRCVDALRI
VIMPHIEFEH IDIFLDCLSN TKRY
//
