MFNA_METJA
ID MFNA_METJA Reviewed; 396 AA.
AC Q60358;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=L-tyrosine/L-aspartate decarboxylase {ECO:0000305};
DE Short=TDC/ADC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000305};
DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24891443};
DE EC=4.1.1.25 {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:15715981};
GN Name=mfnA {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000303|PubMed:15715981};
GN OrderedLocusNames=MJ0050;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A TYROSINE DECARBOXYLASE, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=15715981; DOI=10.1016/j.bbagen.2004.12.003;
RA Kezmarsky N.D., Xu H., Graham D.E., White R.H.;
RT "Identification and characterization of a L-tyrosine decarboxylase in
RT Methanocaldococcus jannaschii.";
RL Biochim. Biophys. Acta 1722:175-182(2005).
RN [3]
RP FUNCTION AS AN ASPARTATE DECARBOXYLASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=24891443; DOI=10.1128/jb.01784-14;
RA Wang Y., Xu H., White R.H.;
RT "Beta-alanine biosynthesis in Methanocaldococcus jannaschii.";
RL J. Bacteriol. 196:2869-2875(2014).
RN [4] {ECO:0007744|PDB:3F9T}
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of L-tyrosine decarboxylase MfnA (EC 4.1.1.25)
RT (NP_247014.1) from Methanococcus jannaschii at 2.11 A resolution.";
RL Submitted (NOV-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce
CC tyramine for methanofuran biosynthesis (PubMed:15715981). Can also
CC catalyze the decarboxylation of L-aspartate to produce beta-alanine for
CC coenzyme A (CoA) biosynthesis (PubMed:24891443).
CC {ECO:0000269|PubMed:15715981, ECO:0000269|PubMed:24891443}.
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, ECO:0000269|PubMed:15715981};
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, ECO:0000269|PubMed:24891443};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01610,
CC ECO:0000269|PubMed:15715981};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine and O-
CC methylhydroxylamine. {ECO:0000269|PubMed:15715981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for L-tyrosine {ECO:0000269|PubMed:15715981};
CC KM=0.8 mM for L-aspartate {ECO:0000269|PubMed:24891443};
CC pH dependence:
CC Optimum pH is 7.5-8.5 for tyrosine decarboxylase activity.
CC {ECO:0000269|PubMed:15715981};
CC Temperature dependence:
CC Thermostable. Retains full tyrosine decarboxylase activity after
CC heating at 100 degrees Celsius for 10 minutes and 42% of its activity
CC after 10 minutes at 110 degrees Celsius. Inactive after 10 minutes at
CC 121 degrees Celsius. {ECO:0000269|PubMed:15715981};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:15715981}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24891443}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15715981}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. MfnA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01610}.
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DR EMBL; L77117; AAB98031.1; -; Genomic_DNA.
DR PIR; B64306; B64306.
DR PDB; 3F9T; X-ray; 2.11 A; A/B=1-396.
DR PDB; 6JY1; X-ray; 1.72 A; A=1-396.
DR PDB; 6LDR; X-ray; 1.79 A; A=1-396.
DR PDB; 6LDS; X-ray; 1.80 A; A=1-396.
DR PDB; 6LDT; X-ray; 1.93 A; A=1-396.
DR PDB; 6M4Y; X-ray; 2.10 A; A=1-396.
DR PDBsum; 3F9T; -.
DR PDBsum; 6JY1; -.
DR PDBsum; 6LDR; -.
DR PDBsum; 6LDS; -.
DR PDBsum; 6LDT; -.
DR PDBsum; 6M4Y; -.
DR AlphaFoldDB; Q60358; -.
DR SMR; Q60358; -.
DR STRING; 243232.MJ_0050; -.
DR EnsemblBacteria; AAB98031; AAB98031; MJ_0050.
DR KEGG; mja:MJ_0050; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_028929_2_1_2; -.
DR InParanoid; Q60358; -.
DR OMA; DPHKMGL; -.
DR PhylomeDB; Q60358; -.
DR BioCyc; MetaCyc:MON-12228; -.
DR BRENDA; 4.1.1.11; 3260.
DR BRENDA; 4.1.1.25; 3260.
DR UniPathway; UPA00080; -.
DR UniPathway; UPA00241; -.
DR EvolutionaryTrace; Q60358; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0004837; F:tyrosine decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:2001120; P:methanofuran biosynthetic process; TAS:UniProtKB.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..396
FT /note="L-tyrosine/L-aspartate decarboxylase"
FT /id="PRO_0000147023"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610,
FT ECO:0000269|Ref.4"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 94..114
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6JY1"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6JY1"
FT TURN 243..247
FT /evidence="ECO:0007829|PDB:6LDR"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:3F9T"
FT HELIX 289..326
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:6JY1"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:6JY1"
FT HELIX 380..393
FT /evidence="ECO:0007829|PDB:6JY1"
SQ SEQUENCE 396 AA; 45050 MW; 41CB8DEE45A8BBC0 CRC64;
MRNMQEKGVS EKEILEELKK YRSLDLKYED GNIFGSMCSN VLPITRKIVD IFLETNLGDP
GLFKGTKLLE EKAVALLGSL LNNKDAYGHI VSGGTEANLM ALRCIKNIWR EKRRKGLSKN
EHPKIIVPIT AHFSFEKGRE MMDLEYIYAP IKEDYTIDEK FVKDAVEDYD VDGIIGIAGT
TELGTIDNIE ELSKIAKENN IYIHVDAAFG GLVIPFLDDK YKKKGVNYKF DFSLGVDSIT
IDPHKMGHCP IPSGGILFKD IGYKRYLDVD APYLTETRQA TILGTRVGFG GACTYAVLRY
LGREGQRKIV NECMENTLYL YKKLKENNFK PVIEPILNIV AIEDEDYKEV CKKLRDRGIY
VSVCNCVKAL RIVVMPHIKR EHIDNFIEIL NSIKRD
