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Q8FU86

- PAND_COREF

UniProt

Q8FU86 - PAND_COREF

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Protein

Aspartate 1-decarboxylase

Gene
panD, CE0135
Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity.UniRule annotation

Catalytic activityi

L-aspartate = beta-alanine + CO2.UniRule annotation

Cofactori

Pyruvoyl group By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251Schiff-base intermediate with substrate; via pyruvic acid By similarity
Binding sitei57 – 571Substrate By similarity
Active sitei58 – 581Proton donor By similarity

GO - Molecular functioni

  1. aspartate 1-decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. alanine biosynthetic process Source: InterPro
  2. pantothenate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate 1-decarboxylase (EC:4.1.1.11)
Alternative name(s):
Aspartate alpha-decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Name:panD
Ordered Locus Names:CE0135
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2424Aspartate 1-decarboxylase beta chain By similarityPRO_0000023065Add
BLAST
Chaini25 – 136112Aspartate 1-decarboxylase alpha chain By similarityPRO_0000023066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyruvic acid (Ser) By similarity

Post-translational modificationi

Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus By similarity.UniRule annotation

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits By similarity.

Protein-protein interaction databases

STRINGi196164.CE0135.

Structurei

3D structure databases

ProteinModelPortaliQ8FU86.
SMRiQ8FU86. Positions 1-113.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 753Substrate binding By similarity

Sequence similaritiesi

Belongs to the PanD family.

Phylogenomic databases

HOGENOMiHOG000221007.
KOiK01579.
OMAiELMIHIM.
OrthoDBiEOG6P5ZMC.

Family and domain databases

HAMAPiMF_00446. PanD.
InterProiIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERiPTHR21012. PTHR21012. 1 hit.
PfamiPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF006246. Asp_decarbox. 1 hit.
ProDomiPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR00223. panD. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8FU86-1 [UniParc]FASTAAdd to Basket

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MLRTILGSKI HRATVTQADL DYVGSITIDA DLVNAAGLIE GEKVAVVDIT    50
NGARIETYVI TGDAGTGSIC INGAAAHLIN PGDLVIIMSY LQATDAEARA 100
YQPNIVHVDA DNRIVALGND AGEPIPGSSL LSSRSL 136
Length:136
Mass (Da):14,098
Last modified:March 1, 2003 - v1
Checksum:i9C5042CB497CCC3D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC16945.1.
RefSeqiNP_736745.1. NC_004369.1.
WP_006768557.1. NZ_GG700684.1.

Genome annotation databases

EnsemblBacteriaiBAC16945; BAC16945; BAC16945.
GeneIDi1031997.
KEGGicef:CE0135.
PATRICi21486458. VBICorEff9312_0183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC16945.1 .
RefSeqi NP_736745.1. NC_004369.1.
WP_006768557.1. NZ_GG700684.1.

3D structure databases

ProteinModelPortali Q8FU86.
SMRi Q8FU86. Positions 1-113.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE0135.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC16945 ; BAC16945 ; BAC16945 .
GeneIDi 1031997.
KEGGi cef:CE0135.
PATRICi 21486458. VBICorEff9312_0183.

Phylogenomic databases

HOGENOMi HOG000221007.
KOi K01579.
OMAi ELMIHIM.
OrthoDBi EOG6P5ZMC.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00002 .

Family and domain databases

HAMAPi MF_00446. PanD.
InterProi IPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view ]
PANTHERi PTHR21012. PTHR21012. 1 hit.
Pfami PF02261. Asp_decarbox. 1 hit.
[Graphical view ]
PIRSFi PIRSF006246. Asp_decarbox. 1 hit.
ProDomi PD009294. Asp_decarbox. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR00223. panD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiPAND_COREF
AccessioniPrimary (citable) accession number: Q8FU86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 80 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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