ID MFNA_METB6 Reviewed; 365 AA.
AC A7IAB9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Mboo_2166;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS56680.1; -; Genomic_DNA.
DR RefSeq; WP_012107738.1; NC_009712.1.
DR AlphaFoldDB; A7IAB9; -.
DR SMR; A7IAB9; -.
DR STRING; 456442.Mboo_2166; -.
DR GeneID; 5411277; -.
DR KEGG; mbn:Mboo_2166; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_028929_2_1_2; -.
DR OrthoDB; 56891at2157; -.
DR UniPathway; UPA00080; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002408; 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 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.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..365
FT /note="Probable L-tyrosine/L-aspartate decarboxylase"
FT /id="PRO_0000323513"
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ SEQUENCE 365 AA; 39263 MW; 27412A7B427031DA CRC64;
MLSNGISEDD LFSFLSLHKK EDLDHRYILS SMCTLPHPVA VRAHCMFMET NLGDPGLFPG
TAALERLLVE RLGTLFHHKN AGGYATSGGT ESNIQALRLA KALRPGSSPN VVLPESVHFS
FKKACDLLSL EMRSVPLGTD RRIMADKAAE LIDKNTICLV GVAGTTEYGM VDPIADLAKI
AAQQDIFLHV DAAFGGMVIP FLPKPVPFDF ALPGVTTLAV DPHKMGMSTI PAGVLLTREP
DMLDALNIDT PYLTVKKGYT LGGTRPGAPM AGALAVLDYL GISGMKAVVA GCMKNTERLI
AGMETRGIQP AASPDVNVAT FVCDRVPEPW KVSWTRAGHL RIVCMPHVTA DRIEAFLSDF
GDMYA
//
