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Protein

Probable rhamnogalacturonate lyase A

Gene

rglA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 2 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:AO090011000349
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiFungiDB:AO090011000349.

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 – 528508Probable rhamnogalacturonate lyase APRO_0000394369Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ2U0Q1.
SMRiQ2U0Q1. Positions 21-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171008.
KOiK18195.
OMAiQPTGFRN.
OrthoDBiEOG092C31LY.

Family and domain databases

CDDicd10316. RGL4_M. 1 hit.
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.

Q2U0Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRTILFST SFLWVRVANA AFGITTSDDS YVIDAGSANP LKFTVSRSSC
60 70 80 90 100
DITSINYYGS ELQYSGTGSH IGSGLGSADV SAVEDGDYIK VTCDTDTLTQ
110 120 130 140 150
YFVVHNGDSV IHMATYTTEE PSVGELRFIA RLNSELLPNE EPFGDVSTTS
160 170 180 190 200
GGEAIEGSDV FLVDGETRSK FYSSQRFIDD QRHCVAGDAH RVCMILNQYE
210 220 230 240 250
TSSGGPFFRD INSNNGGSYN SLYWYMNSGH VQTEDRRQGL HGPYSMYFSR
260 270 280 290 300
SGTPSTDIDT SFFANLDIKG YVATDGRGTV SGTASGADSS FKWVVHWYNA
310 320 330 340 350
DAQYWTYTSS DGSFTSPAMK PGDYTMVYYQ GEYKVAETSV SVTVGSSTSK
360 370 380 390 400
DISGSVETGD TIFKIGDWDG TPTGFRNAEN QLRMHPSDSR MSSWGPLTYT
410 420 430 440 450
VGSSELTDFP MAAFKGVNDP VTIKFTATSA QTGAATLRIG TTLSFAGGRP
460 470 480 490 500
QATINDYEGS APSAPTNLNS RGVTRGAYRG LGEVYDVNIP SGTIVEGENT
510 520
ITISVISGSS GDEFLAPNFI FDCVELFQ
Length:528
Mass (Da):56,966
Last modified:January 24, 2006 - v1
Checksum:iE13D69616194B4BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007171 Genomic DNA. Translation: BAE64864.1.
RefSeqiXP_001825997.1. XM_001825945.1.

Genome annotation databases

EnsemblFungiiCADAORAT00005112; CADAORAP00005022; CADAORAG00005112.
GeneIDi5998100.
KEGGiaor:AOR_1_590054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007171 Genomic DNA. Translation: BAE64864.1.
RefSeqiXP_001825997.1. XM_001825945.1.

3D structure databases

ProteinModelPortaliQ2U0Q1.
SMRiQ2U0Q1. Positions 21-528.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00005112; CADAORAP00005022; CADAORAG00005112.
GeneIDi5998100.
KEGGiaor:AOR_1_590054.

Organism-specific databases

EuPathDBiFungiDB:AO090011000349.

Phylogenomic databases

HOGENOMiHOG000171008.
KOiK18195.
OMAiQPTGFRN.
OrthoDBiEOG092C31LY.

Family and domain databases

CDDicd10316. RGL4_M. 1 hit.
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...

Entry informationi

Entry nameiRGLA_ASPOR
AccessioniPrimary (citable) accession number: Q2U0Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: September 7, 2016
This is version 54 of the entry and version 1 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.