L-tyrosine decarboxylase - Methanocaldococcus jannaschii

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Reviewed, UniProtKB/Swiss-Prot Q60358 (MFNA_METJA)

Last modified December 15, 2009. Version 60. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    L-tyrosine decarboxylase
      Short name=TDC
    EC=4.1.1.25

Gene names

Name:	mfnA
Ordered Locus Names:	MJ0050

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

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Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Specifically catalyzes the decarboxylation of L-tyrosine to produce tyramine. Ref.2
Catalytic activity	L-tyrosine = tyramine + CO₂. HAMAP MF_01610
Cofactor	Pyridoxal phosphate. Ref.2
Enzyme regulation	Inhibited by hydroxylamine and O-methylhydroxylamine. HAMAP MF_01610
Pathway	Cofactor biosynthesis; methanofuran biosynthesis. HAMAP MF_01610
Subunit structure	Homodimer. HAMAP MF_01610
Sequence similarities	Belongs to the group II decarboxylase family. Archaeal L-tyrosine decarboxylase subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=1.6 mM for L-tyrosine HAMAP MF_01610 pH dependence: Optimum pH is 7.5-8.5. Temperature dependence: Thermostable. Retains full activity after heating at 100 degrees Celsius for 10 minutes and 42% of its activity after 10 minutes at 110 degrees Celsius. Inactive after 10 minutes at 121 degrees Celsius.

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Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro carboxylic acid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	pyridoxal phosphate binding Inferred from electronic annotation. Source: HAMAP transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro tyrosine decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

L-tyrosine decarboxylase HAMAP MF_01610

PRO_0000147023

Amino acid modifications

Modified residue

245

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

396

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q60358-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 41CB8DEE45A8BBC0
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FASTA

396

45,050

        10         20         30         40         50         60 
MRNMQEKGVS EKEILEELKK YRSLDLKYED GNIFGSMCSN VLPITRKIVD IFLETNLGDP 

        70         80         90        100        110        120 
GLFKGTKLLE EKAVALLGSL LNNKDAYGHI VSGGTEANLM ALRCIKNIWR EKRRKGLSKN 

       130        140        150        160        170        180 
EHPKIIVPIT AHFSFEKGRE MMDLEYIYAP IKEDYTIDEK FVKDAVEDYD VDGIIGIAGT 

       190        200        210        220        230        240 
TELGTIDNIE ELSKIAKENN IYIHVDAAFG GLVIPFLDDK YKKKGVNYKF DFSLGVDSIT 

       250        260        270        280        290        300 
IDPHKMGHCP IPSGGILFKD IGYKRYLDVD APYLTETRQA TILGTRVGFG GACTYAVLRY 

       310        320        330        340        350        360 
LGREGQRKIV NECMENTLYL YKKLKENNFK PVIEPILNIV AIEDEDYKEV CKKLRDRGIY 

       370        380        390 
VSVCNCVKAL RIVVMPHIKR EHIDNFIEIL NSIKRD

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Identification and characterization of a L-tyrosine decarboxylase in Methanocaldococcus jannaschii." Kezmarsky N.D., Xu H., Graham D.E., White R.H. Biochim. Biophys. Acta 1722:175-182(2005) [PubMed: 15715981] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, COFACTOR. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

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Cross-references

Sequence databases

L77117 Genomic DNA. Translation: AAB98031.1.

PIR

B64306.

RefSeq

NP_247014.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3F9T	X-ray	2.11	A/B	1-396	[»]

ModBase

Search...

Genome annotation databases

GeneID

1450889.

GenomeReviews

Gene locus MJ0050 in contig L77117_GR.

KEGG

mja:MJ0050.

NMPDR

fig|243232.1.peg.51.

TIGR

MJ0050.

Phylogenomic databases

HOGENOM

HBG497871.

OMA

NLGDPGL.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12228.

BRENDA

4.1.1.25. 256362.

Family and domain databases

HAMAP

MF_01610.
[Tree]

InterPro

IPR004839. Aminotransferase_I/II.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase_major.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

PANTHER

PTHR11999. Pyridoxal_deC. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
PF00282. Pyridoxal_deC. 1 hit.
[Graphical view]

PROSITE

PS00392. DDC_GAD_HDC_YDC. False negative.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

MFNA_METJA

Accession

Primary (citable) accession number: Q60358

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	December 15, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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