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Protein

Rhamnogalacturonate lyase A

Gene

rglA

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.3 Publications

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.

pH dependencei

Optimum pH is 6.0, enzymatic activity becomes unstable below this value.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16403.
BRENDAi4.2.2.23. 488.

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhamnogalacturonate lyase A (EC:4.2.2.23)
Alternative name(s):
Rhamnogalacturonan lyase
Gene namesi
Name:rglA
Synonyms:RGL4
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi169K → A: Impairs enzyme activity. 1
Mutagenesisi229H → A: Impairs enzyme activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
ChainiPRO_000002491220 – 527Rhamnogalacturonate lyase AAdd BLAST508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 92
Disulfide bondi183 ↔ 192
Glycosylationi350N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ00019.

Structurei

Secondary structure

1527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 25Combined sources4
Beta strandi27 – 33Combined sources7
Beta strandi40 – 45Combined sources6
Turni46 – 48Combined sources3
Beta strandi51 – 56Combined sources6
Beta strandi64 – 66Combined sources3
Beta strandi68 – 70Combined sources3
Beta strandi78 – 84Combined sources7
Beta strandi87 – 93Combined sources7
Beta strandi95 – 104Combined sources10
Beta strandi109 – 118Combined sources10
Beta strandi125 – 131Combined sources7
Turni133 – 135Combined sources3
Beta strandi138 – 140Combined sources3
Helixi143 – 146Combined sources4
Beta strandi152 – 155Combined sources4
Turni156 – 158Combined sources3
Beta strandi159 – 162Combined sources4
Beta strandi165 – 168Combined sources4
Helixi169 – 172Combined sources4
Helixi176 – 178Combined sources3
Beta strandi180 – 185Combined sources6
Beta strandi190 – 194Combined sources5
Beta strandi212 – 214Combined sources3
Beta strandi219 – 226Combined sources8
Beta strandi238 – 250Combined sources13
Helixi260 – 264Combined sources5
Helixi273 – 275Combined sources3
Beta strandi277 – 286Combined sources10
Beta strandi292 – 297Combined sources6
Beta strandi302 – 306Combined sources5
Beta strandi312 – 314Combined sources3
Beta strandi320 – 329Combined sources10
Beta strandi332 – 341Combined sources10
Beta strandi346 – 348Combined sources3
Beta strandi359 – 365Combined sources7
Beta strandi367 – 370Combined sources4
Helixi377 – 380Combined sources4
Beta strandi397 – 399Combined sources3
Turni400 – 402Combined sources3
Helixi405 – 407Combined sources3
Beta strandi408 – 413Combined sources6
Turni414 – 416Combined sources3
Beta strandi420 – 426Combined sources7
Helixi428 – 430Combined sources3
Beta strandi434 – 444Combined sources11
Beta strandi448 – 453Combined sources6
Helixi472 – 474Combined sources3
Beta strandi483 – 488Combined sources6
Beta strandi495 – 505Combined sources11
Helixi512 – 514Combined sources3
Beta strandi515 – 526Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NKGX-ray1.50A20-527[»]
2XHNX-ray1.52A/B20-527[»]
3NJVX-ray2.40A20-527[»]
3NJXX-ray1.94A20-527[»]
ProteinModelPortaliQ00019.
SMRiQ00019.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00019.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK18195.

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.

Q00019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKASLLSFV AFTAQVAHAA FGITTSSSAY VIDTNAPNQL KFTVSRSSCD
60 70 80 90 100
ITSIIHYGTE LQYSSQGSHI GSGLGSATVT ATQSGDYIKV TCVTDTLTQY
110 120 130 140 150
MVVHNGDPII HMATYITAEP SIGELRFIAR LNSDLLPNEE PFGDVSTTAD
160 170 180 190 200
GTAIEGSDVF LVGSETRSKF YSSERFIDDQ RHCIAGDAHR VCMILNQYES
210 220 230 240 250
SSGGPFHRDI NSNNGGSYNA LYWYMNSGHV QTESYRMGLH GPYSMYFSRS
260 270 280 290 300
GTPSTSIDTS FFADLDIKGY VAASGRGKVA GTASGADSSM DWVVHWYNDA
310 320 330 340 350
AQYWTYTSSS GSFTSPAMKP GTYTMVYYQG EYAVATSSVT VSAGSTTTKN
360 370 380 390 400
ISGSVKTGTT IFKIGEWDGQ PTGFRNAANQ LRMHPSDSRM SSWGPLTYTV
410 420 430 440 450
GSSALTDFPM AVFKSVNNPV TIKFTATSAQ TGAATLRIGT TLSFAGGRPQ
460 470 480 490 500
ATINSYTGSA PAAPTNLDSR GVTRGAYRGL GEVYDVSIPS GTIVAGTNTI
510 520
TINVISGSSG DTYLSPNFIF DCVELFQ
Length:527
Mass (Da):56,190
Last modified:November 1, 1996 - v1
Checksum:iB0E14412E5CDC080
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35500 mRNA. Translation: AAA64368.1.
PIRiB55415.

Genome annotation databases

KEGGiag:AAA64368.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35500 mRNA. Translation: AAA64368.1.
PIRiB55415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NKGX-ray1.50A20-527[»]
2XHNX-ray1.52A/B20-527[»]
3NJVX-ray2.40A20-527[»]
3NJXX-ray1.94A20-527[»]
ProteinModelPortaliQ00019.
SMRiQ00019.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

Proteomic databases

PRIDEiQ00019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA64368.

Phylogenomic databases

KOiK18195.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16403.
BRENDAi4.2.2.23. 488.

Miscellaneous databases

EvolutionaryTraceiQ00019.

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_ASPAC
AccessioniPrimary (citable) accession number: Q00019
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 80 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.