ID G0H1D8_METMI Unreviewed; 384 AA.
AC G0H1D8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 ORFNames=GYY_00665 {ECO:0000313|EMBL:AEK19023.1};
OS Methanococcus maripaludis X1.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=1053692 {ECO:0000313|Proteomes:UP000008889};
RN [1] {ECO:0000313|EMBL:AEK19023.1, ECO:0000313|Proteomes:UP000008889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1 {ECO:0000313|EMBL:AEK19023.1,
RC ECO:0000313|Proteomes:UP000008889};
RX PubMed=21914896; DOI=10.1128/JB.05835-11;
RA Wang X., Greenfield P., Li D., Hendry P., Volk H., Sutherland T.D.;
RT "Complete Genome Sequence of a Nonculturable Methanococcus maripaludis
RT Strain Extracted in a Metagenomic Survey of Petroleum Reservoir Fluids.";
RL J. Bacteriol. 193:5595-5595(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|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; CP002913; AEK19023.1; -; Genomic_DNA.
DR RefSeq; WP_013998596.1; NC_015847.1.
DR AlphaFoldDB; G0H1D8; -.
DR GeneID; 10981561; -.
DR KEGG; mmd:GYY_00665; -.
DR PATRIC; fig|1053692.7.peg.134; -.
DR HOGENOM; CLU_028929_2_1_2; -.
DR UniPathway; UPA00080; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000008889; 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}.
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01610,
FT ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 384 AA; 43108 MW; E126C718614AF5D2 CRC64;
MDEQDILNEL REYRNQDLKY EEGYILGSMC TKPHPIARKI SEMFFETNLG DPGLFKGTSK
LEKEVVSMIG GILHNKNAFG YIISGGTEAN LTAMRAFKNI SKSKGKPQNI IIPETAHFSF
DKAKDMMDLN VVRPPLTKYF TMDVKFIQDY IEDSKNEVSG IVGIAGCTEL GSIDNICELS
KIAVENDILL HVDAAFGGFV IPFLDDKYKL KGYNYDFDFS LNGVSSITID PHKMGLAPIS
AGGILFKDNT FKKYLDVDAP YLTEKQQATI IGTRSGVGVA STWGIMKLLG IEGYKKLVNE
SMEKTTHLVK KAREYGFETA IDPVMNIVAL KDENKHETCM KLREENWYVS VCRCVDALRI
VVMPHLEIEH IDGFLESLSN TKKY
//
