ID F0T911_METLA Unreviewed; 392 AA.
AC F0T911;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=Metbo_0381 {ECO:0000313|EMBL:ADZ08633.1};
OS Methanobacterium lacus (strain AL-21).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=877455 {ECO:0000313|EMBL:ADZ08633.1, ECO:0000313|Proteomes:UP000007490};
RN [1] {ECO:0000313|Proteomes:UP000007490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL-21 {ECO:0000313|Proteomes:UP000007490};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. AL-21.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADZ08633.1, ECO:0000313|Proteomes:UP000007490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL-21 {ECO:0000313|EMBL:ADZ08633.1,
RC ECO:0000313|Proteomes:UP000007490};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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; CP002551; ADZ08633.1; -; Genomic_DNA.
DR RefSeq; WP_013643984.1; NC_015216.1.
DR AlphaFoldDB; F0T911; -.
DR STRING; 877455.Metbo_0381; -.
DR GeneID; 10276818; -.
DR KEGG; mel:Metbo_0381; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_028929_2_1_2; -.
DR OrthoDB; 56891at2157; -.
DR UniPathway; UPA00080; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000007490; 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 {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:UP000007490}.
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01610,
FT ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 392 AA; 43498 MW; 1B02DDB6035C56E9 CRC64;
MEDKGRSETE IFDELHQFKT RDMTHRSGKI LGSMCTCPHP IGLNAFKMFL ESNLGDPGLF
KGTQAMEDEV ISSLGELLGE RDVYGHIITG GTEANIMAMR AARNTFKHNY PDCEDVNIVV
PKSAHFSFKK AADMLCLDLL EAELDENYRV DINSLDELIN ENTAAVVAIA GTTELGKIDP
VEKISELCLK RGVYLHVDAA FGGYSIPFLN EMGYDLPNFD FSLPGVCSIT IDPHKMGLAP
IPTGGILFRK KTFLESISIE TPYLTEDRQS TIVGTRTGAS TAATWALMNY LGKEGYRKVS
KECMEITELL HRGVVEAGFN PVTEPELNIV AFTSDEMTVD EIADGLERSG WAVSISSYPR
AIRIIVMPHV KEEHVELLLD DLRELRSLHS KE
//
