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Protein

Oligoxyloglucan reducing end-specific cellobiohydrolase

Gene
N/A
Organism
Geotrichum sp. (strain M128)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.1 Publication

pH dependencei

Optimum pH is 3.5-5.0 with the oligoxyloglucan heptasaccharide XXXG as a substrate. Over 90% activity is retained between pH 4.8 and 8.0.1 Publication

Temperature dependencei

Optimum temperature is 50-60 degrees Celsius with the oligoxyloglucan heptasaccharide XXXG as a substrate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581Nucleophile1 Publication
Active sitei488 – 4881Proton donor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16634.
BRENDAi3.2.1.150. 2419.
3.2.1.91. 2419.

Protein family/group databases

CAZyiGH74. Glycoside Hydrolase Family 74.
mycoCLAPiXBH74A_GEOSP.

Names & Taxonomyi

Protein namesi
Recommended name:
Oligoxyloglucan reducing end-specific cellobiohydrolase1 PublicationImported (EC:3.2.1.150)
Short name:
OXG-RCBH1 Publication
OrganismiGeotrichum sp. (strain M128)
Taxonomic identifieri203496 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeGeotrichum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581D → N: No catalytic activity. 1 Publication
Mutagenesisi467 – 4671E → Q: No effect on catalytic activity. 1 Publication
Mutagenesisi488 – 4881D → N: No catalytic activity. 1 Publication
Mutagenesisi513 – 5131D → N: No effect on catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 812789Oligoxyloglucan reducing end-specific cellobiohydrolase1 PublicationPRO_0000395429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence analysis
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence analysis
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence analysis
Glycosylationi563 – 5631N-linked (GlcNAc...)Sequence analysis
Glycosylationi697 – 6971N-linked (GlcNAc...)Sequence analysis
Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence analysis
Glycosylationi754 – 7541N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
812
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314Combined sources
Beta strandi40 – 456Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 608Combined sources
Beta strandi62 – 665Combined sources
Turni67 – 704Combined sources
Beta strandi71 – 755Combined sources
Helixi81 – 866Combined sources
Beta strandi88 – 958Combined sources
Beta strandi98 – 1069Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi125 – 1317Combined sources
Turni141 – 1444Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi155 – 1628Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1736Combined sources
Beta strandi179 – 1813Combined sources
Turni190 – 1923Combined sources
Beta strandi194 – 1996Combined sources
Beta strandi207 – 2137Combined sources
Beta strandi217 – 2226Combined sources
Helixi239 – 2435Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi264 – 27411Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi285 – 2895Combined sources
Turni290 – 2923Combined sources
Beta strandi295 – 2973Combined sources
Turni302 – 3043Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi319 – 3268Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi349 – 3546Combined sources
Beta strandi357 – 3615Combined sources
Helixi362 – 3665Combined sources
Beta strandi376 – 3783Combined sources
Helixi379 – 3813Combined sources
Helixi391 – 3977Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi433 – 4364Combined sources
Beta strandi441 – 4455Combined sources
Helixi447 – 4526Combined sources
Beta strandi458 – 4603Combined sources
Beta strandi469 – 4746Combined sources
Beta strandi477 – 49014Combined sources
Beta strandi492 – 4954Combined sources
Beta strandi510 – 5178Combined sources
Beta strandi525 – 5295Combined sources
Beta strandi542 – 55110Combined sources
Beta strandi571 – 5744Combined sources
Beta strandi581 – 5844Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi608 – 6103Combined sources
Beta strandi618 – 6203Combined sources
Beta strandi622 – 6243Combined sources
Beta strandi628 – 6325Combined sources
Beta strandi635 – 6417Combined sources
Beta strandi644 – 6496Combined sources
Beta strandi665 – 6673Combined sources
Beta strandi671 – 6755Combined sources
Turni676 – 6783Combined sources
Beta strandi679 – 6857Combined sources
Beta strandi691 – 6955Combined sources
Beta strandi697 – 7037Combined sources
Beta strandi721 – 7288Combined sources
Beta strandi733 – 7408Combined sources
Beta strandi758 – 7636Combined sources
Beta strandi771 – 7788Combined sources
Beta strandi780 – 7845Combined sources
Beta strandi796 – 7994Combined sources
Beta strandi804 – 8063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SQJX-ray2.20A/B24-812[»]
2EBSX-ray2.40A/B24-812[»]
ProteinModelPortaliQ8J0D2.
SMRiQ8J0D2. Positions 27-809.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8J0D2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati118 – 12811BNR 1Sequence analysisAdd
BLAST
Repeati218 – 22811BNR 2Sequence analysisAdd
BLAST
Repeati350 – 36011BNR 3Sequence analysisAdd
BLAST
Repeati595 – 60511BNR 4Sequence analysisAdd
BLAST
Repeati637 – 64610BNR 5Sequence analysis
Repeati681 – 69111BNR 6Sequence analysisAdd
BLAST
Repeati736 – 74611BNR 7Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 74 family.1 Publication
Contains 7 BNR repeats.Sequence analysis

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

KOiK18651.

Family and domain databases

InterProiIPR002860. BNR_rpt.
[Graphical view]
PfamiPF15899. BNR_6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8J0D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAVTSLGKA LTALSILASL AVAKEHYEFK NVAIGGGGYI TGIVAHPKTK
60 70 80 90 100
DLLYARTDIG GAYRWDAGTS KWIPLNDFIE AQDMNIMGTE SIALDPNNPD
110 120 130 140 150
RLYLAQGRYV GDEWAAFYVS EDRGQSFTIY ESPFPMGAND MGRNNGERLA
160 170 180 190 200
VNPFNSNEVW MGTRTEGIWK SSDRAKTWTN VTSIPDAFTN GIGYTSVIFD
210 220 230 240 250
PERNGTIYAS ATAPQGMYVT HDGGVSWEPV AGQPSSWLNR TTGAFPDKKP
260 270 280 290 300
ASIAPQPMKV ALTPNFLYVT YADYPGPWGV TFGEVWRQNR TSGAWDDITP
310 320 330 340 350
RVGNSSPAPY NNQTFPAGGF CGLSVDATNP NRLVVITLDR DPGPALDSIY
360 370 380 390 400
LSTDAGATWK DVTQLSSPSN LEGNWGHPTN AARYKDGTPV PWLDFNNGPQ
410 420 430 440 450
WGGYGAPHGT PGLTKFGWWM SAVLIDPFNP EHLMYGTGAT IWATDTLSRV
460 470 480 490 500
EKDWAPSWYL QIDGIEENAI LSLRSPKSGA ALLSGIGDIS GMKHDDLTKP
510 520 530 540 550
QKMFGAPQFS NLDSIDAAGN FPNVVVRAGS SGHEYDSACA RGAYATDGGD
560 570 580 590 600
AWTIFPTCPP GMNASHYQGS TIAVDASGSQ IVWSTKLDEQ ASGPWYSHDY
610 620 630 640 650
GKTWSVPAGD LKAQTANVLS DKVQDGTFYA TDGGKFFVST DGGKSYAAKG
660 670 680 690 700
AGLVTGTSLM PAVNPWVAGD VWVPVPEGGL FHSTDFGASF TRVGTANATL
710 720 730 740 750
VSVGAPKSKS DGKKASAPSA VFIWGTDKPG SDIGLYRSDD NGSTWTRVND
760 770 780 790 800
QEHNYSGPTM IEADPKVYGR VYLGTNGRGI VYADLTNKKS NEEKSTAKCA
810
NGQKGTHCYV KK
Length:812
Mass (Da):87,081
Last modified:March 1, 2003 - v1
Checksum:iF5C740F32D8B17E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB089343 mRNA. Translation: BAC22065.1.

Genome annotation databases

KEGGiag:BAC22065.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB089343 mRNA. Translation: BAC22065.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SQJX-ray2.20A/B24-812[»]
2EBSX-ray2.40A/B24-812[»]
ProteinModelPortaliQ8J0D2.
SMRiQ8J0D2. Positions 27-809.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH74. Glycoside Hydrolase Family 74.
mycoCLAPiXBH74A_GEOSP.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAC22065.

Phylogenomic databases

KOiK18651.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16634.
BRENDAi3.2.1.150. 2419.
3.2.1.91. 2419.

Miscellaneous databases

EvolutionaryTraceiQ8J0D2.

Family and domain databases

InterProiIPR002860. BNR_rpt.
[Graphical view]
PfamiPF15899. BNR_6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBHRE_GEOS1
AccessioniPrimary (citable) accession number: Q8J0D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 50 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, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.