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Protein

Arylmalonate decarboxylase

Gene
N/A
Organism
Bordetella bronchiseptica (Alcaligenes bronchisepticus)
Status
Reviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2-aryl-2-methylmalonate = 2-arylpropanoate + CO2.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Enzyme and pathway databases

BRENDAi4.1.1.76. 227.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylmalonate decarboxylase (EC:4.1.1.76)
Short name:
AMDase
OrganismiBordetella bronchiseptica (Alcaligenes bronchisepticus)
Taxonomic identifieri518 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000645761 – 240Arylmalonate decarboxylaseAdd BLAST240

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 15Combined sources8
Helixi23 – 27Combined sources5
Beta strandi33 – 37Combined sources5
Helixi39 – 41Combined sources3
Helixi45 – 51Combined sources7
Helixi52 – 54Combined sources3
Helixi55 – 64Combined sources10
Beta strandi67 – 72Combined sources6
Helixi75 – 79Combined sources5
Helixi83 – 97Combined sources15
Beta strandi101 – 103Combined sources3
Helixi104 – 114Combined sources11
Beta strandi118 – 126Combined sources9
Helixi128 – 140Combined sources13
Beta strandi144 – 150Combined sources7
Helixi156 – 160Combined sources5
Helixi164 – 176Combined sources13
Beta strandi182 – 187Combined sources6
Beta strandi189 – 191Combined sources3
Helixi196 – 204Combined sources9
Beta strandi208 – 210Combined sources3
Helixi211 – 222Combined sources12
Beta strandi231 – 233Combined sources3
Helixi235 – 238Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VLBX-ray1.92A/B/C/D1-240[»]
3DG9X-ray1.50A1-240[»]
3DTVX-ray2.10A/B/C/D1-240[»]
3EISX-ray2.10A/B/C/D1-240[»]
3IP8X-ray1.50A1-240[»]
3IXLX-ray1.45A1-240[»]
3IXMX-ray1.90A1-240[»]
ProteinModelPortaliQ05115.
SMRiQ05115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05115.

Family & Domainsi

Phylogenomic databases

KOiK06033.

Family and domain databases

InterProiIPR026286. MaiA/AMDase.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PIRSFiPIRSF015736. MI. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05115-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQASTPTIG MIVPPAAGLV PADGARLYPD LPFIASGLGL GSVTPEGYDA
60 70 80 90 100
VIESVVDHAR RLQKQGAAVV SLMGTSLSFY RGAAFNAALT VAMREATGLP
110 120 130 140 150
CTTMSTAVLN GLRALGVRRV ALATAYIDDV NERLAAFLAE ESLVPTGCRS
160 170 180 190 200
LGITGVEAMA RVDTATLVDL CVRAFEAAPD SDGILLSCGG LLTLDAIPEV
210 220 230 240
ERRLGVPVVS SSPAGFWDAV RLAGGGAKAR PGYGRLFDES
Length:240
Mass (Da):24,735
Last modified:February 1, 1995 - v1
Checksum:i2514373725BDAA7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S54007 Genomic DNA. Translation: AAC60426.1.
D13116 Genomic DNA. Translation: BAA02419.1.
PIRiA48374. JS0754.
RefSeqiWP_059373149.1. NZ_BBVB01000006.1.

Genome annotation databases

KEGGiag:AAC60426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S54007 Genomic DNA. Translation: AAC60426.1.
D13116 Genomic DNA. Translation: BAA02419.1.
PIRiA48374. JS0754.
RefSeqiWP_059373149.1. NZ_BBVB01000006.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VLBX-ray1.92A/B/C/D1-240[»]
3DG9X-ray1.50A1-240[»]
3DTVX-ray2.10A/B/C/D1-240[»]
3EISX-ray2.10A/B/C/D1-240[»]
3IP8X-ray1.50A1-240[»]
3IXLX-ray1.45A1-240[»]
3IXMX-ray1.90A1-240[»]
ProteinModelPortaliQ05115.
SMRiQ05115.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC60426.

Phylogenomic databases

KOiK06033.

Enzyme and pathway databases

BRENDAi4.1.1.76. 227.

Miscellaneous databases

EvolutionaryTraceiQ05115.

Family and domain databases

InterProiIPR026286. MaiA/AMDase.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PIRSFiPIRSF015736. MI. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMDA_BORBO
AccessioniPrimary (citable) accession number: Q05115
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 61 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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 one 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.