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Protein

Pyruvoyl-dependent arginine decarboxylase 2

Gene

pdaD2

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

pyruvateBy similarityNote: Binds 1 pyruvoyl group covalently per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei40 – 412Cleavage (non-hydrolytic)By similarity

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

BioCyciMMAZ192952:GCK2-2654-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvoyl-dependent arginine decarboxylase 2 (EC:4.1.1.19)
Short name:
PvlArgDC 2
Cleaved into the following 2 chains:
Gene namesi
Name:pdaD2
Ordered Locus Names:MM_2595
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000000595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4040Pyruvoyl-dependent arginine decarboxylase 2 subunit betaBy similarityPRO_0000023320Add
BLAST
Chaini41 – 183143Pyruvoyl-dependent arginine decarboxylase 2 subunit alphaBy similarityPRO_0000023321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Pyruvic acid (Ser)By similarity

Interactioni

Protein-protein interaction databases

STRINGi192952.MM_2595.

Structurei

3D structure databases

ProteinModelPortaliP58890.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdaD family.Curated

Phylogenomic databases

eggNOGiCOG1945.
HOGENOMiHOG000012204.
KOiK02626.
OMAiSEHHSFG.

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.

P58890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPRKAFLTK GTGVHKDRLA SFELALRDAK IEKYNLVSVS SILPPNCKLV
60 70 80 90 100
PREEGLAELK PGAIVHCVLA RNDTNEPHRL MASAIGTAVP VNEENYGYIS
110 120 130 140 150
EHHSFGEEEI IAGEYAEDLA ATMLATTLGI EFDAEMAWHE REQVYKASGH
160 170 180
IFDTFHMCQT AKGDKDGKWT TTVAAMVFVT SKC
Length:183
Mass (Da):20,211
Last modified:July 11, 2002 - v1
Checksum:iEC848E8E644A2360
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM32291.1.
RefSeqiNP_634619.1. NC_003901.1.
WP_011034508.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM32291; AAM32291; MM_2595.
GeneIDi1480937.
KEGGimma:MM_2595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM32291.1.
RefSeqiNP_634619.1. NC_003901.1.
WP_011034508.1. NC_003901.1.

3D structure databases

ProteinModelPortaliP58890.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192952.MM_2595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM32291; AAM32291; MM_2595.
GeneIDi1480937.
KEGGimma:MM_2595.

Phylogenomic databases

eggNOGiCOG1945.
HOGENOMiHOG000012204.
KOiK02626.
OMAiSEHHSFG.

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-2654-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. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiPDAD2_METMA
AccessioniPrimary (citable) accession number: P58890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: February 4, 2015
This is version 78 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.