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A5AA79

- A5AA79_ASPNC

UniProt

A5AA79 - A5AA79_ASPNC

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Protein
Submitted name:

Catalytic activity: L-glutamate = 4-aminobutanoate + CO2

Gene

An02g06860

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Unreviewed - Annotation score: 1 out of 5- Protein inferred from homologyi

Functioni

Cofactori

Pyridoxal phosphate.UniRule annotation

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. carboxylic acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Names & Taxonomyi

Protein namesi
Submitted name:
Catalytic activity: L-glutamate = 4-aminobutanoate + CO2Imported (EC:4.1.1.15Imported)
Gene namesi
ORF Names:An02g06860Imported
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)Imported
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 4R

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00002141.

Structurei

3D structure databases

ProteinModelPortaliA5AA79.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000005382.
KOiK01580.
OrthoDBiEOG7380F0.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

A5AA79-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASAPPASRA DEVQNLLRAV EDLLIPFIRS ADEDPLPQQS LHNGINGDSQ
60 70 80 90 100
PRGTSLVEHK KPEELQKLLQ LDLPDQGTGQ DGLIDVLRKV LRYSVNTWHQ
110 120 130 140 150
GFLDKLYAST NAPGVASELI LAALNTNVHV YQVSPALTVI EKHTGKQLAS
160 170 180 190 200
LFGLNGPRAG GISVQGGSAS NTTSIVIARN NLYPSTKKDG NGNYRFVLFT
210 220 230 240 250
SAHGHYSIEK AAQMLGLGSS SVWAVPIDKQ GRMIPSELEA LVQKALAEDR
260 270 280 290 300
TPFYVNATAG TTVMGSFDPF HEIADICKKY NLWFHVDGSW GGSFIFSSEQ
310 320 330 340 350
RAKLSGAEKA DSIAINPHKM LGVPVTCSFL LAADIRRFHL ANTLPAGYLF
360 370 380 390 400
HNEDTAAAPD TLNGETELVV DSPEVWDLAD LTLQCGRRAD SLKLFLSWTY
410 420 430 440 450
YGTAGYERQI DSACAVAAHL ATLVEQNPNF VLVSENPPPC LQVCFHYAPN
460 470 480 490 500
RAFVHPRGLV SNETERGKAN SKVTEQITHT IVNKGFMVDF APPSGDEDAV
510 520 530 540 550
GNGKFFRCVV NVQTTRETVE ALIRAIEEVG PGIVERLKRE SAGEVSTRRL
560
GERGHGPVVH H
Length:561
Mass (Da):61,021
Last modified:June 12, 2007 - v1
Checksum:iF43C1BE38BD40DB4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270015 Genomic DNA. Translation: CAK44231.1.
RefSeqiXP_001399821.1. XM_001399784.2.

Genome annotation databases

EnsemblFungiiCADANGAT00002203; CADANGAP00002141; CADANGAG00002203.
GeneIDi4979176.
KEGGiang:ANI_1_944024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270015 Genomic DNA. Translation: CAK44231.1 .
RefSeqi XP_001399821.1. XM_001399784.2.

3D structure databases

ProteinModelPortali A5AA79.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00002141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00002203 ; CADANGAP00002141 ; CADANGAG00002203 .
GeneIDi 4979176.
KEGGi ang:ANI_1_944024.

Phylogenomic databases

HOGENOMi HOG000005382.
KOi K01580.
OrthoDBi EOG7380F0.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513Imported.

Entry informationi

Entry nameiA5AA79_ASPNC
AccessioniPrimary (citable) accession number: A5AA79
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: October 1, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3