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A3DLU8

- ARGDC_STAMF

UniProt

A3DLU8 - ARGDC_STAMF

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Protein
Arginine decarboxylase proenzyme
Gene
Smar_0500
Organism
Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity By similarity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Pyruvoyl group By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei71 – 722Cleavage (non-hydrolytic); by autolysis By similarity
Active sitei72 – 721Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active sitei77 – 771Proton acceptor; for processing activity By similarity
Active sitei92 – 921Proton donor; for catalytic activity By similarity

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. arginine catabolic process Source: UniProtKB-HAMAP
  2. polyamine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciSMAR399550:GHK2-502-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase proenzyme (EC:4.1.1.19)
Short name:
ADC
Short name:
ArgDC
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Ordered Locus Names:Smar_0500
OrganismiStaphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1)
Taxonomic identifieri399550 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeStaphylothermus
ProteomesiUP000000254: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7171Arginine decarboxylase beta chain By similarity
PRO_0000364125Add
BLAST
Chaini72 – 12756Arginine decarboxylase alpha chain By similarity
PRO_0000364126Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721Pyruvic acid (Ser); by autocatalysis By similarity

Post-translational modificationi

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain By similarity.UniRule annotation

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers By similarity.

Protein-protein interaction databases

STRINGi399550.Smar_0500.

Structurei

3D structure databases

ProteinModelPortaliA3DLU8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiHIANMHL.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A3DLU8-1 [UniParc]FASTAAdd to Basket

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MDNTLIDPRI IGKHVYGNLY EIPEEIAGDE EYLRNVVVEA AKLANMTLLE    50
VKSWKLGGEK GGVSVIALVL ESHIAIHTWI NYRYATVDVY TCGEKSDPWR 100
AFNYIVEKLK PKEYTVNYAD RTQLLKQ 127
Length:127
Mass (Da):14,547
Last modified:March 20, 2007 - v1
Checksum:iAA1932B4F767B069
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000575 Genomic DNA. Translation: ABN69608.1.
RefSeqiYP_001040516.1. NC_009033.1.

Genome annotation databases

EnsemblBacteriaiABN69608; ABN69608; Smar_0500.
GeneIDi4907823.
KEGGismr:Smar_0500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000575 Genomic DNA. Translation: ABN69608.1 .
RefSeqi YP_001040516.1. NC_009033.1.

3D structure databases

ProteinModelPortali A3DLU8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 399550.Smar_0500.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN69608 ; ABN69608 ; Smar_0500 .
GeneIDi 4907823.
KEGGi smr:Smar_0500.

Phylogenomic databases

eggNOGi COG1586.
HOGENOMi HOG000216579.
KOi K01611.
OMAi HIANMHL.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SMAR399550:GHK2-502-MONOMER.

Family and domain databases

Gene3Di 3.60.90.10. 1 hit.
HAMAPi MF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProi IPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view ]
Pfami PF02675. AdoMet_dc. 1 hit.
[Graphical view ]
SUPFAMi SSF56276. SSF56276. 1 hit.
TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota."
    Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N.
    BMC Genomics 10:145-145(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43588 / DSM 3639 / F1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43588 / DSM 3639 / F1.

Entry informationi

Entry nameiARGDC_STAMF
AccessioniPrimary (citable) accession number: A3DLU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 50 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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