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Database: UniProt
Entry: D3DZR8_METRM
LinkDB: D3DZR8_METRM
Original site: D3DZR8_METRM 
ID   D3DZR8_METRM            Unreviewed;       388 AA.
AC   D3DZR8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
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:ADC47746.1};
GN   OrderedLocusNames=mru_1896 {ECO:0000313|EMBL:ADC47746.1};
OS   Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS   OCM 146 / M1) (Methanobacterium ruminantium).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC47746.1, ECO:0000313|Proteomes:UP000008680};
RN   [1] {ECO:0000313|EMBL:ADC47746.1, ECO:0000313|Proteomes:UP000008680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1
RC   {ECO:0000313|Proteomes:UP000008680};
RX   PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA   Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA   Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA   Janssen P.H., Dey D., Attwood G.T.;
RT   "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT   reveals new possibilities for controlling ruminant methane emissions.";
RL   PLoS ONE 5:E8926-E8926(2010).
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|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01610, 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}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC       1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR   EMBL; CP001719; ADC47746.1; -; Genomic_DNA.
DR   RefSeq; WP_012956694.1; NC_013790.1.
DR   AlphaFoldDB; D3DZR8; -.
DR   STRING; 634498.mru_1896; -.
DR   GeneID; 8771566; -.
DR   KEGG; mru:mru_1896; -.
DR   PATRIC; fig|634498.28.peg.1896; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   OrthoDB; 56891at2157; -.
DR   UniPathway; UPA00080; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000008680; 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 {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01610};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, 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:UP000008680}.
FT   MOD_RES         234
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01610,
FT                   ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   388 AA;  42773 MW;  7BA42C0D373AD2DA CRC64;
     MNKEPISEEE IFKELDFYQS QDCKYSDGRI LGSMCTQAHP IAQKAFIQFL ESNLGDPGLF
     KGTKAIEDKV LKMIGSFLSI ENPVGHIVTG GTEANIMAIR AARNIARDEK GISQGEIIVP
     QSAHFSFKKA SDILNLKLRE IVLDDSYQLD ASFVEDEINE NTVAIVGVAG TTELGMIDPI
     EELSNIALEN NIHLHVDAAF GGFSIPFLKE IGYGLPEFDF SLKGVKSITV DPHKMGLAPI
     PAGGILFRNE EYLDSISVNS PYLTIKHQST IVGTRMGATS AATFAVMKYL GKDGYARLAK
     ESLDNAIFLA ESVKQLGYEL VVEPKLNIVA FNHPKLETDD LAQLIEKRDW KVSCSSCPKA
     IRVILMNHIK REHIVELISD LKDISESI
//
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