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Protein

Probable pyruvoyl-dependent arginine decarboxylase

Gene

pdaD

Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
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
Sitei42 – 432Cleavage (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

BioCyciPAES290512:GHUT-729-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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:Paes_0705
OrganismiProsthecochloris aestuarii (strain DSM 271 / SK 413)
Taxonomic identifieri290512 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris
ProteomesiUP000002725: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4242Pyruvoyl-dependent arginine decarboxylase subunit betaUniRule annotationPRO_1000145474Add
BLAST
Chaini43 – 181139Pyruvoyl-dependent arginine decarboxylase subunit alphaUniRule annotationPRO_1000145475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Pyruvic acid (Ser)UniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi290512.Paes_0705.

Structurei

3D structure databases

ProteinModelPortaliB4S6J7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdaD family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1945.
HOGENOMiHOG000012204.
KOiK02626.
OMAiSEHHSFG.
OrthoDBiEOG6JHRMR.

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.

B4S6J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFVPTKVFF TKGVGRHKEY LSSFELALRE AKIEKCNLVT VSSIFPPQCE
60 70 80 90 100
RISVEEGLKS LSPGEITFAV MARNSTNEHG RLIASSIGVA LPADESVYGY
110 120 130 140 150
LSEHHPYGQT EEQSGEYAED LAATMLATTL GIEFDPNKDW DEREGIYKMS
160 170 180
GKIINSFNIT QSAEGQNGLW TTVIACAVLL P
Length:181
Mass (Da):19,898
Last modified:September 23, 2008 - v1
Checksum:i968B05A7649D11F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF45752.1.
RefSeqiWP_012505289.1. NC_011059.1.
YP_002015399.1. NC_011059.1.

Genome annotation databases

EnsemblBacteriaiACF45752; ACF45752; Paes_0705.
GeneIDi6458504.
KEGGipaa:Paes_0705.
PATRICi23041096. VBIProAes37017_0736.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF45752.1.
RefSeqiWP_012505289.1. NC_011059.1.
YP_002015399.1. NC_011059.1.

3D structure databases

ProteinModelPortaliB4S6J7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290512.Paes_0705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF45752; ACF45752; Paes_0705.
GeneIDi6458504.
KEGGipaa:Paes_0705.
PATRICi23041096. VBIProAes37017_0736.

Phylogenomic databases

eggNOGiCOG1945.
HOGENOMiHOG000012204.
KOiK02626.
OMAiSEHHSFG.
OrthoDBiEOG6JHRMR.

Enzyme and pathway databases

BioCyciPAES290512:GHUT-729-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. "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 271 / SK 413.

Entry informationi

Entry nameiPDAD_PROA2
AccessioniPrimary (citable) accession number: B4S6J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: March 4, 2015
This is version 41 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.