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Protein

Probable rhamnogalacturonate lyase A

Gene

rglA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity).By similarity

Catalytic activityi

Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable rhamnogalacturonate lyase A (EC:4.2.2.23)
Gene namesi
Name:rglA
ORF Names:An14g01130
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006706 Componenti: Chromosome 1R

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 531511Probable rhamnogalacturonate lyase APRO_5000220898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 93By similarity
Disulfide bondi184 ↔ 193By similarity

Keywords - PTMi

Disulfide bond

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171008.
OrthoDBiEOG7034SR.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR014766. CarboxyPept_regulatory_dom.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. GH-type_carb-bd.
IPR029413. RG-lyase_II.
IPR029411. RG-lyase_III.
IPR016590. Rhamnogalacturonase_B.
IPR015364. RhgB_N.
[Graphical view]
PfamiPF14683. CBM-like. 1 hit.
PF14686. fn3_3. 1 hit.
PF09284. RhgB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF011794. Rhamnogalacturonase_B. 1 hit.
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF74650. SSF74650. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A2R2L1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKTSLLSL LSLAAGVVNA DFGITTNDDS YVINANSPNS LVFTVDRGSC
60 70 80 90 100
DITSIVHYGT ELQYSGKGSH IGSGLGTATV SATKSGDYIK VTCETDTLTQ
110 120 130 140 150
YMVVHDGDPI IHMATYITEE PSIGELRFIA RLNSDVLPNE EPFGDVSNTA
160 170 180 190 200
DGEAIEGSDV FLVDGETRSK FYSSQRFIDD QRHCIAGDEH RVCMILNQYE
210 220 230 240 250
TSSGGPFHRD INSNNGGDYN SLYWYMNSGH VQLESYRMGL HGPYSMYFSR
260 270 280 290 300
SGTPSTDIDT SFFADLDIEG YVAESGRGTV SGTASGADSS FDWVVHWYND
310 320 330 340 350
DAQYWTYTSS SGSFTSPAMK PGTYTMVYYQ GEYVVATSEV TVSAGSSTSK
360 370 380 390 400
DISGSVETGT TIFKIGDWDG QPTGFRNAEN QLRMHPSDSR MSDWGPLTYT
410 420 430 440 450
VGSSSLTDFP MAIFKSVNSP VTIKFTATSD QTGAATLRIG TTLSFAGGRP
460 470 480 490 500
QATINDYEGS APSAPTNLDS RGVTRGAYRG YGDVYDVSVP EGTIVEGENT
510 520 530
ITISVISGSS GDDFLSPNFL DAVFIIALVD N
Length:531
Mass (Da):57,138
Last modified:May 18, 2010 - v2
Checksum:iB9FAC68AAE5D74CF
GO

Sequence cautioni

The sequence CAK46452.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270312 Genomic DNA. Translation: CAK46452.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270312 Genomic DNA. Translation: CAK46452.1. Sequence problems.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000171008.
OrthoDBiEOG7034SR.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR014766. CarboxyPept_regulatory_dom.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. GH-type_carb-bd.
IPR029413. RG-lyase_II.
IPR029411. RG-lyase_III.
IPR016590. Rhamnogalacturonase_B.
IPR015364. RhgB_N.
[Graphical view]
PfamiPF14683. CBM-like. 1 hit.
PF14686. fn3_3. 1 hit.
PF09284. RhgB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF011794. Rhamnogalacturonase_B. 1 hit.
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

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 A1513.

Entry informationi

Entry nameiRGLA_ASPNC
AccessioniPrimary (citable) accession number: A2R2L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.