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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)DescriptionActionsGraphical viewLength
Active sitei58Nucleophile1 Publication1
Active sitei488Proton donor1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi58D → N: No catalytic activity. 1 Publication1
Mutagenesisi467E → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi488D → N: No catalytic activity. 1 Publication1
Mutagenesisi513D → N: No effect on catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000039542924 – 812Oligoxyloglucan reducing end-specific cellobiohydrolase1 PublicationAdd BLAST789

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi180N-linked (GlcNAc...)Sequence analysis1
Glycosylationi204N-linked (GlcNAc...)Sequence analysis1
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Glycosylationi289N-linked (GlcNAc...)Sequence analysis1
Glycosylationi312N-linked (GlcNAc...)Sequence analysis1
Glycosylationi563N-linked (GlcNAc...)Sequence analysis1
Glycosylationi697N-linked (GlcNAc...)Sequence analysis1
Glycosylationi741N-linked (GlcNAc...)Sequence analysis1
Glycosylationi754N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1812
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 31Combined sources4
Beta strandi40 – 45Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi53 – 60Combined sources8
Beta strandi62 – 66Combined sources5
Turni67 – 70Combined sources4
Beta strandi71 – 75Combined sources5
Helixi81 – 86Combined sources6
Beta strandi88 – 95Combined sources8
Beta strandi98 – 106Combined sources9
Beta strandi116 – 122Combined sources7
Beta strandi125 – 131Combined sources7
Turni141 – 144Combined sources4
Beta strandi149 – 152Combined sources4
Beta strandi155 – 162Combined sources8
Beta strandi164 – 166Combined sources3
Beta strandi168 – 173Combined sources6
Beta strandi179 – 181Combined sources3
Turni190 – 192Combined sources3
Beta strandi194 – 199Combined sources6
Beta strandi207 – 213Combined sources7
Beta strandi217 – 222Combined sources6
Helixi239 – 243Combined sources5
Beta strandi251 – 254Combined sources4
Beta strandi256 – 262Combined sources7
Beta strandi264 – 274Combined sources11
Beta strandi276 – 278Combined sources3
Beta strandi285 – 289Combined sources5
Turni290 – 292Combined sources3
Beta strandi295 – 297Combined sources3
Turni302 – 304Combined sources3
Beta strandi305 – 307Combined sources3
Beta strandi319 – 326Combined sources8
Beta strandi329 – 338Combined sources10
Beta strandi349 – 354Combined sources6
Beta strandi357 – 361Combined sources5
Helixi362 – 366Combined sources5
Beta strandi376 – 378Combined sources3
Helixi379 – 381Combined sources3
Helixi391 – 397Combined sources7
Beta strandi413 – 416Combined sources4
Beta strandi423 – 425Combined sources3
Beta strandi433 – 436Combined sources4
Beta strandi441 – 445Combined sources5
Helixi447 – 452Combined sources6
Beta strandi458 – 460Combined sources3
Beta strandi469 – 474Combined sources6
Beta strandi477 – 490Combined sources14
Beta strandi492 – 495Combined sources4
Beta strandi510 – 517Combined sources8
Beta strandi525 – 529Combined sources5
Beta strandi542 – 551Combined sources10
Beta strandi571 – 574Combined sources4
Beta strandi581 – 584Combined sources4
Beta strandi595 – 599Combined sources5
Beta strandi608 – 610Combined sources3
Beta strandi618 – 620Combined sources3
Beta strandi622 – 624Combined sources3
Beta strandi628 – 632Combined sources5
Beta strandi635 – 641Combined sources7
Beta strandi644 – 649Combined sources6
Beta strandi665 – 667Combined sources3
Beta strandi671 – 675Combined sources5
Turni676 – 678Combined sources3
Beta strandi679 – 685Combined sources7
Beta strandi691 – 695Combined sources5
Beta strandi697 – 703Combined sources7
Beta strandi721 – 728Combined sources8
Beta strandi733 – 740Combined sources8
Beta strandi758 – 763Combined sources6
Beta strandi771 – 778Combined sources8
Beta strandi780 – 784Combined sources5
Beta strandi796 – 799Combined sources4
Beta strandi804 – 806Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8J0D2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati118 – 128BNR 1Sequence analysisAdd BLAST11
Repeati218 – 228BNR 2Sequence analysisAdd BLAST11
Repeati350 – 360BNR 3Sequence analysisAdd BLAST11
Repeati595 – 605BNR 4Sequence analysisAdd BLAST11
Repeati637 – 646BNR 5Sequence analysis10
Repeati681 – 691BNR 6Sequence analysisAdd BLAST11
Repeati736 – 746BNR 7Sequence analysisAdd BLAST11

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SQJX-ray2.20A/B24-812[»]
2EBSX-ray2.40A/B24-812[»]
ProteinModelPortaliQ8J0D2.
SMRiQ8J0D2.
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: November 2, 2016
This is version 52 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.