CBHRE_GEOS1
ID CBHRE_GEOS1 Reviewed; 812 AA.
AC Q8J0D2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Oligoxyloglucan reducing end-specific cellobiohydrolase {ECO:0000303|PubMed:12374797, ECO:0000312|EMBL:BAC22065.1};
DE Short=OXG-RCBH {ECO:0000303|PubMed:12374797};
DE EC=3.2.1.150;
DE Flags: Precursor;
OS Geotrichum sp. (strain M128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum; unclassified Geotrichum.
OX NCBI_TaxID=203496;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC22065.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-42; 51-62; 715-726 AND
RP 767-775, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12374797; DOI=10.1074/jbc.m208443200;
RA Yaoi K., Mitsuishi Y.;
RT "Purification, characterization, cloning, and expression of a novel
RT xyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific
RT cellobiohydrolase.";
RL J. Biol. Chem. 277:48276-48281(2002).
RN [2] {ECO:0000305, ECO:0000312|PDB:1SQJ}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 24-812, ACTIVE SITES, AND
RP MUTAGENESIS OF ASP-58; GLU-467; ASP-488 AND ASP-513.
RX PubMed=15242597; DOI=10.1016/j.str.2004.04.020;
RA Yaoi K., Kondo H., Noro N., Suzuki M., Tsuda S., Mitsuishi Y.;
RT "Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan
RT reducing-end-specific cellobiohydrolase.";
RL Structure 12:1209-1217(2004).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-812 IN COMPLEX WITH
RP HEPTAXYLOGLUCAN.
RX PubMed=17498741; DOI=10.1016/j.jmb.2007.04.035;
RA Yaoi K., Kondo H., Hiyoshi A., Noro N., Sugimoto H., Tsuda S.,
RA Mitsuishi Y., Miyazaki K.;
RT "The structural basis for the exo-mode of action in GH74 oligoxyloglucan
RT reducing end-specific cellobiohydrolase.";
RL J. Mol. Biol. 370:53-62(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of cellobiose from the reducing end of xyloglucans
CC consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl
CC groups on O-6 of the glucose residues. To be a substrate, the first
CC residue must be unsubstituted, the second residue may bear a xylosyl
CC group, whether further glycosylated or not, and the third residue,
CC which becomes the new terminus by the action of the enzyme, is
CC preferably xylosylated, but this xylose residue must not be further
CC substituted.; EC=3.2.1.150; Evidence={ECO:0000269|PubMed:12374797};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.5-5.0 with the oligoxyloglucan heptasaccharide XXXG
CC as a substrate. Over 90% activity is retained between pH 4.8 and 8.0.
CC {ECO:0000269|PubMed:12374797};
CC Temperature dependence:
CC Optimum temperature is 50-60 degrees Celsius with the oligoxyloglucan
CC heptasaccharide XXXG as a substrate. {ECO:0000269|PubMed:12374797};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000269|PubMed:12374797}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB089343; BAC22065.1; -; mRNA.
DR PDB; 1SQJ; X-ray; 2.20 A; A/B=24-812.
DR PDB; 2EBS; X-ray; 2.40 A; A/B=24-812.
DR PDBsum; 1SQJ; -.
DR PDBsum; 2EBS; -.
DR AlphaFoldDB; Q8J0D2; -.
DR SMR; Q8J0D2; -.
DR CAZy; GH74; Glycoside Hydrolase Family 74.
DR CLAE; XBH74A_GEOSP; -.
DR KEGG; ag:BAC22065; -.
DR BioCyc; MetaCyc:MON-16634; -.
DR BRENDA; 3.2.1.150; 2419.
DR EvolutionaryTrace; Q8J0D2; -.
DR GO; GO:0033945; F:oligoxyloglucan reducing-end-specific cellobiohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR002860; BNR_rpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF15899; BNR_6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:12374797"
FT CHAIN 24..812
FT /note="Oligoxyloglucan reducing end-specific
FT cellobiohydrolase"
FT /evidence="ECO:0000269|PubMed:12374797"
FT /id="PRO_0000395429"
FT REPEAT 118..128
FT /note="BNR 1"
FT /evidence="ECO:0000255"
FT REPEAT 218..228
FT /note="BNR 2"
FT /evidence="ECO:0000255"
FT REPEAT 350..360
FT /note="BNR 3"
FT /evidence="ECO:0000255"
FT REPEAT 595..605
FT /note="BNR 4"
FT /evidence="ECO:0000255"
FT REPEAT 637..646
FT /note="BNR 5"
FT /evidence="ECO:0000255"
FT REPEAT 681..691
FT /note="BNR 6"
FT /evidence="ECO:0000255"
FT REPEAT 736..746
FT /note="BNR 7"
FT /evidence="ECO:0000255"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:15242597"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15242597"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 58
FT /note="D->N: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:15242597"
FT MUTAGEN 467
FT /note="E->Q: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:15242597"
FT MUTAGEN 488
FT /note="D->N: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:15242597"
FT MUTAGEN 513
FT /note="D->N: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:15242597"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1SQJ"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1SQJ"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1SQJ"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1SQJ"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1SQJ"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1SQJ"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1SQJ"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:1SQJ"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:1SQJ"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:1SQJ"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:1SQJ"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 477..490
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 542..551
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 635..641
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 644..649
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:1SQJ"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 691..695
FT /evidence="ECO:0007829|PDB:2EBS"
FT STRAND 697..703
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 721..728
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 733..740
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 758..763
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 771..778
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 780..784
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:1SQJ"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:1SQJ"
SQ SEQUENCE 812 AA; 87081 MW; F5C740F32D8B17E5 CRC64;
MVAVTSLGKA LTALSILASL AVAKEHYEFK NVAIGGGGYI TGIVAHPKTK DLLYARTDIG
GAYRWDAGTS KWIPLNDFIE AQDMNIMGTE SIALDPNNPD RLYLAQGRYV GDEWAAFYVS
EDRGQSFTIY ESPFPMGAND MGRNNGERLA VNPFNSNEVW MGTRTEGIWK SSDRAKTWTN
VTSIPDAFTN GIGYTSVIFD PERNGTIYAS ATAPQGMYVT HDGGVSWEPV AGQPSSWLNR
TTGAFPDKKP ASIAPQPMKV ALTPNFLYVT YADYPGPWGV TFGEVWRQNR TSGAWDDITP
RVGNSSPAPY NNQTFPAGGF CGLSVDATNP NRLVVITLDR DPGPALDSIY LSTDAGATWK
DVTQLSSPSN LEGNWGHPTN AARYKDGTPV PWLDFNNGPQ WGGYGAPHGT PGLTKFGWWM
SAVLIDPFNP EHLMYGTGAT IWATDTLSRV EKDWAPSWYL QIDGIEENAI LSLRSPKSGA
ALLSGIGDIS GMKHDDLTKP QKMFGAPQFS NLDSIDAAGN FPNVVVRAGS SGHEYDSACA
RGAYATDGGD AWTIFPTCPP GMNASHYQGS TIAVDASGSQ IVWSTKLDEQ ASGPWYSHDY
GKTWSVPAGD LKAQTANVLS DKVQDGTFYA TDGGKFFVST DGGKSYAAKG AGLVTGTSLM
PAVNPWVAGD VWVPVPEGGL FHSTDFGASF TRVGTANATL VSVGAPKSKS DGKKASAPSA
VFIWGTDKPG SDIGLYRSDD NGSTWTRVND QEHNYSGPTM IEADPKVYGR VYLGTNGRGI
VYADLTNKKS NEEKSTAKCA NGQKGTHCYV KK
