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A8MBV3

- ARGDC_CALMQ

UniProt

A8MBV3 - ARGDC_CALMQ

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Protein

Arginine decarboxylase proenzyme

Gene

Cmaq_0451

Organism
Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)
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.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Pyruvoyl group.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei81 – 822Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei82 – 821Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei87 – 871Proton acceptor; for processing activityUniRule annotation
Active sitei102 – 1021Proton donor; for catalytic activityUniRule annotation

GO - Molecular functioni

  1. adenosylmethionine decarboxylase activity Source: InterPro
  2. arginine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

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

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciCMAQ397948:GH9M-462-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase proenzymeUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
ADCUniRule annotation
Short name:
ArgDCUniRule annotation
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylaseUniRule annotation
Cleaved into the following 2 chains:
Arginine decarboxylase beta chainUniRule annotation
Arginine decarboxylase alpha chainUniRule annotation
Gene namesi
Ordered Locus Names:Cmaq_0451
OrganismiCaldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)
Taxonomic identifieri397948 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeCaldivirga
ProteomesiUP000001137: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181Arginine decarboxylase beta chainUniRule annotationPRO_0000364111Add
BLAST
Chaini82 – 13453Arginine decarboxylase alpha chainUniRule annotationPRO_0000364112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Pyruvic acid (Ser); by autocatalysisUniRule annotation

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.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.UniRule annotation

Protein-protein interaction databases

STRINGi397948.Cmaq_0451.

Structurei

3D structure databases

ProteinModelPortaliA8MBV3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiHILAEMY.

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.

A8MBV3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLQQQESPIP RLGVGEEGVV GRHVFGEVWG VNDKLLQDDE YLKNLVIKAA
60 70 80 90 100
EVANMHLVDV KVWRFGGGDK GGVSVIALVL ESHIAIHTWP AYNYATIDVY
110 120 130
TCGEHSRPWD AYDYIIKQLN PKTFTKTIVD RSSK
Length:134
Mass (Da):15,053
Last modified:December 4, 2007 - v1
Checksum:iBFFCD14C36EE792E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000852 Genomic DNA. Translation: ABW01296.1.
RefSeqiYP_001540286.1. NC_009954.1.

Genome annotation databases

EnsemblBacteriaiABW01296; ABW01296; Cmaq_0451.
GeneIDi5709779.
KEGGicma:Cmaq_0451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000852 Genomic DNA. Translation: ABW01296.1 .
RefSeqi YP_001540286.1. NC_009954.1.

3D structure databases

ProteinModelPortali A8MBV3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 397948.Cmaq_0451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABW01296 ; ABW01296 ; Cmaq_0451 .
GeneIDi 5709779.
KEGGi cma:Cmaq_0451.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci CMAQ397948:GH9M-462-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700844 / DSM 13496 / JCM 10307 / IC-167.

Entry informationi

Entry nameiARGDC_CALMQ
AccessioniPrimary (citable) accession number: A8MBV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: December 4, 2007
Last modified: October 1, 2014
This is version 46 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3