(data stored in ACNUC10043 zone)

SWISSPROT: D1YVJ9_METPS

ID   D1YVJ9_METPS            Unreviewed;       377 AA.
AC   D1YVJ9;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 56.
DE   RecName: Full=Probable L-tyrosine/L-aspartate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01610};
DE            Short=TDC/ADC {ECO:0000256|HAMAP-Rule:MF_01610};
DE            EC=4.1.1.11 {ECO:0000256|HAMAP-Rule:MF_01610};
DE            EC=4.1.1.25 {ECO:0000256|HAMAP-Rule:MF_01610};
GN   Name=mfnA {ECO:0000256|HAMAP-Rule:MF_01610,
GN   ECO:0000313|EMBL:BAI60471.1};
GN   OrderedLocusNames=MCP_0399 {ECO:0000313|EMBL:BAI60471.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60471.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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:0000256|HAMAP-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:0000256|HAMAP-
CC         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:0000256|HAMAP-
CC         Rule:MF_01610};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01610,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01610}.
CC   -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01610}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. MfnA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01610}.
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DR   EMBL; AP011532; BAI60471.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0399; -.
DR   EnsemblBacteria; BAI60471; BAI60471; MCP_0399.
DR   KEGG; mpd:MCP_0399; -.
DR   PATRIC; fig|304371.9.peg.409; -.
DR   eggNOG; arCOG00027; Archaea.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000246269; -.
DR   KO; K18933; -.
DR   OMA; DPHKMGL; -.
DR   UniPathway; UPA00080; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001882; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVJ9.
DR   SWISS-2DPAGE; D1YVJ9.
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01610};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01610};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01610,
KW   ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01610,
FT                   ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   377 AA;  41299 MW;  D957BFA823859978 CRC64;
     MREHGVDEDT IIRELKGACA RNVPYERVLS SMCTTPHPIA IKAHKEFIVS NLGDPRLFPG
     TASLEHACIG MLGELLHLPS AVGYITTGGT ESNIQALRTA RQLKHVDPGK ANIVLPESAH
     YSFDKAAQML GVSLRRTPLD DEMKADMDAM AGLVDKNTIA LVAVAGTTEF GQVDPIPAIS
     KLALDENIFL HVDAAFGGFV IPFMKDPSKY RFDFELPGVM SIAIDPHKMG MSTIPSGGLL
     YRDERHMKSL EISAQYLTSQ VQSSLAGTRT GASAAATYAV MRHLGMDGYR RVVSECMDNT
     MFLRDSLVDM DIELALEPIM NIVTAKLPDA QSTRKKLCDM GWFVSTTSRP EALRMVVMPH
     VTRDVIEAFM ADLKKIS
//

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