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A3CWM4 (MFNA_METMJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-tyrosine decarboxylase

Short name=TDC
EC=4.1.1.25
Gene names
Name:mfnA
Ordered Locus Names:Memar_1848
OrganismMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]
Taxonomic identifier368407 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically catalyzes the decarboxylation of L-tyrosine to produce tyramine By similarity. HAMAP-Rule MF_01610

Catalytic activity

L-tyrosine = tyramine + CO2. HAMAP-Rule MF_01610

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01610

Pathway

Cofactor biosynthesis; methanofuran biosynthesis. HAMAP-Rule MF_01610

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01610

Sequence similarities

Belongs to the group II decarboxylase family. Archaeal L-tyrosine decarboxylase subfamily.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcoenzyme biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tyrosine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tyrosine decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365L-tyrosine decarboxylase HAMAP-Rule MF_01610
PRO_0000293185

Amino acid modifications

Modified residue2241N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CWM4 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: BB4D126014B8497B

FASTA36539,401
        10         20         30         40         50         60 
MREVGCPEED LFSFLSSKRR EDLGYRNILS SMCTPPHPVA ARAHAMFLET NLGDPGLFPG 

        70         80         90        100        110        120 
TAALEDLLVR RLGTLMHLPD AGGYATSGGT ESNIQAFRIA KKLKSAKSPN VVVPASSHFS 

       130        140        150        160        170        180 
FTKACDILGL EMRTVPLDAG FRMETEAVDG LIDHNTVALV GVVGTTEYGM VDPISRLSEI 

       190        200        210        220        230        240 
ALDRNVFLHV DAAFGGMVVP FLDRPVPFDF SLPGVSSISV DPHKMGMSTI PAGCLLTRSA 

       250        260        270        280        290        300 
EWFSCLNVDT PYLTVKRECT LAGTRPGASV AAAIAVLEYL GMDGMRAVVA GCMENCRRLI 

       310        320        330        340        350        360 
EGMETLGYPR AVTPDVNVAT FSCERAPVGW RVSTTRNGHM RIVCMPHVTR DVVEQFLVDM 


GDTDA 

« Hide

References

[1]"Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1."
Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. expand/collapse author list , Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:189-196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35101 / DSM 1498 / JR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000562 Genomic DNA. Translation: ABN57774.1.
RefSeqYP_001047756.1. NC_009051.1.

3D structure databases

ProteinModelPortalA3CWM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368407.Memar_1848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN57774; ABN57774; Memar_1848.
GeneID4845930.
KEGGmem:Memar_1848.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000246269.
KOK01592.
OMAKLVWAEL.

Enzyme and pathway databases

BioCycMMAR368407:GH7L-1892-MONOMER.
UniPathwayUPA00080.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_01610. Tyr_decarbox.
InterProIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR021115. Pyridoxal-P_BS.
IPR020931. Tyr_deCO2ase.
[Graphical view]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR03812. tyr_de_CO2_Arch. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMFNA_METMJ
AccessionPrimary (citable) accession number: A3CWM4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways