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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi169 – 1691K → A: Impairs enzyme activity.
Mutagenesisi229 – 2291H → A: Impairs enzyme activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 527508Rhamnogalacturonate lyase APRO_0000024912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 92
Disulfide bondi183 ↔ 192
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources
Beta strandi27 – 337Combined sources
Beta strandi40 – 456Combined sources
Turni46 – 483Combined sources
Beta strandi51 – 566Combined sources
Beta strandi64 – 663Combined sources
Beta strandi68 – 703Combined sources
Beta strandi78 – 847Combined sources
Beta strandi87 – 937Combined sources
Beta strandi95 – 10410Combined sources
Beta strandi109 – 11810Combined sources
Beta strandi125 – 1317Combined sources
Turni133 – 1353Combined sources
Beta strandi138 – 1403Combined sources
Helixi143 – 1464Combined sources
Beta strandi152 – 1554Combined sources
Turni156 – 1583Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi165 – 1684Combined sources
Helixi169 – 1724Combined sources
Helixi176 – 1783Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi219 – 2268Combined sources
Beta strandi238 – 25013Combined sources
Helixi260 – 2645Combined sources
Helixi273 – 2753Combined sources
Beta strandi277 – 28610Combined sources
Beta strandi292 – 2976Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi320 – 32910Combined sources
Beta strandi332 – 34110Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi359 – 3657Combined sources
Beta strandi367 – 3704Combined sources
Helixi377 – 3804Combined sources
Beta strandi397 – 3993Combined sources
Turni400 – 4023Combined sources
Helixi405 – 4073Combined sources
Beta strandi408 – 4136Combined sources
Turni414 – 4163Combined sources
Beta strandi420 – 4267Combined sources
Helixi428 – 4303Combined sources
Beta strandi434 – 44411Combined sources
Beta strandi448 – 4536Combined sources
Helixi472 – 4743Combined sources
Beta strandi483 – 4886Combined sources
Beta strandi495 – 50511Combined sources
Helixi512 – 5143Combined sources
Beta strandi515 – 52612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKGX-ray1.50A20-527[»]
2XHNX-ray1.52A/B20-527[»]
3NJVX-ray2.40A20-527[»]
3NJXX-ray1.94A20-527[»]
ProteinModelPortaliQ00019.
SMRiQ00019. Positions 20-527.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKGX-ray1.50A20-527[»]
2XHNX-ray1.52A/B20-527[»]
3NJVX-ray2.40A20-527[»]
3NJXX-ray1.94A20-527[»]
ProteinModelPortaliQ00019.
SMRiQ00019. Positions 20-527.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL4. Polysaccharide Lyase Family 4.

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: September 7, 2016
This is version 78 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.