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Protein

Pyruvoyl-dependent arginine decarboxylase

Gene

pdaD

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 422Cleavage (non-hydrolytic)UniRule annotation

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyruvate

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-872-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvoyl-dependent arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
PvlArgDCUniRule annotation
Cleaved into the following 2 chains:
Pyruvoyl-dependent arginine decarboxylase subunit betaUniRule annotation
Pyruvoyl-dependent arginine decarboxylase subunit alphaUniRule annotation
Gene namesi
Name:pdaDUniRule annotation
Ordered Locus Names:MTH_870
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4141Pyruvoyl-dependent arginine decarboxylase subunit betaUniRule annotationPRO_0000023324Add
BLAST
Chaini42 – 151110Pyruvoyl-dependent arginine decarboxylase subunit alphaUniRule annotationPRO_0000023325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Pyruvic acid (Ser)UniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi187420.MTH870.

Structurei

3D structure databases

ProteinModelPortaliO26956.
SMRiO26956. Positions 7-41.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdaD family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1945.
KOiK02626.
OMAiMVNCVLS.

Family and domain databases

Gene3Di3.50.20.10. 1 hit.
HAMAPiMF_01404. PvlArgDC.
InterProiIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
PfamiPF01862. PvlArgDC. 1 hit.
[Graphical view]
PIRSFiPIRSF005216. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
ProDomiPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56271. SSF56271. 1 hit.
TIGRFAMsiTIGR00286. TIGR00286. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O26956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIVMKVAIT SGAAEGPTKL NAFDNALLQA GIGDVNLIKV SSILPRNTRI
60 70 80 90 100
VELPELEPGS IVNCVLSHMV SERRGDLISA AVAVATSSDF GCVVENSSVN
110 120 130 140 150
RDPEDVRSEA ISMVRYMMSV RGLEIKELIV EETNHVVEKC GAAVSAVVYL

D
Length:151
Mass (Da):16,114
Last modified:January 1, 1998 - v1
Checksum:i823DD6E28A32E36D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85368.1.
PIRiC69216.
RefSeqiNP_276007.1. NC_000916.1.
WP_010876503.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85368; AAB85368; MTH_870.
GeneIDi1471278.
KEGGimth:MTH870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85368.1.
PIRiC69216.
RefSeqiNP_276007.1. NC_000916.1.
WP_010876503.1. NC_000916.1.

3D structure databases

ProteinModelPortaliO26956.
SMRiO26956. Positions 7-41.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85368; AAB85368; MTH_870.
GeneIDi1471278.
KEGGimth:MTH870.

Phylogenomic databases

eggNOGiCOG1945.
KOiK02626.
OMAiMVNCVLS.

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-872-MONOMER.

Family and domain databases

Gene3Di3.50.20.10. 1 hit.
HAMAPiMF_01404. PvlArgDC.
InterProiIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
PfamiPF01862. PvlArgDC. 1 hit.
[Graphical view]
PIRSFiPIRSF005216. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
ProDomiPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56271. SSF56271. 1 hit.
TIGRFAMsiTIGR00286. TIGR00286. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiPDAD_METTH
AccessioniPrimary (citable) accession number: O26956
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.