XG74_ACET2
ID XG74_ACET2 Reviewed; 842 AA.
AC A3DFA0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Xyloglucanase Xgh74A {ECO:0000250|UniProtKB:Q70DK5};
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=xghA {ECO:0000250|UniProtKB:Q70DK5}; OrderedLocusNames=Cthe_1398;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the glucosidic bonds of unbranched Glc residues in
CC tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. Has low
CC activity on carboxymethylcellulose, lichenan,hydroxyethylcellulose and
CC glucuronoxylan, and no activity on xylan, polygalaturonic acid, wheat
CC arabinoxylan, rhamnogalacturan, curdlan, laminarin, galactomannan,
CC galactan, arabinan and pachyman or amorphous cellulose (By similarity).
CC {ECO:0000250|UniProtKB:Q70DK5}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000250|UniProtKB:Q70DK5}.
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DR EMBL; CP000568; ABN52629.1; -; Genomic_DNA.
DR RefSeq; WP_003518268.1; NC_009012.1.
DR AlphaFoldDB; A3DFA0; -.
DR SMR; A3DFA0; -.
DR STRING; 203119.Cthe_1398; -.
DR CAZy; GH74; Glycoside Hydrolase Family 74.
DR PRIDE; A3DFA0; -.
DR EnsemblBacteria; ABN52629; ABN52629; Cthe_1398.
DR KEGG; cth:Cthe_1398; -.
DR eggNOG; COG4447; Bacteria.
DR HOGENOM; CLU_004180_1_0_9; -.
DR OMA; YSSWWPD; -.
DR OrthoDB; 1293876at2; -.
DR BioCyc; MetaCyc:MON-16464; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00404; Dockerin_1; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..842
FT /note="Xyloglucanase Xgh74A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000225199"
FT REPEAT 134..144
FT /note="BNR 1"
FT /evidence="ECO:0000255"
FT REPEAT 185..196
FT /note="BNR 2"
FT /evidence="ECO:0000255"
FT REPEAT 252..262
FT /note="BNR 3"
FT /evidence="ECO:0000255"
FT REPEAT 358..368
FT /note="BNR 4"
FT /evidence="ECO:0000255"
FT REPEAT 533..541
FT /note="BNR 5"
FT /evidence="ECO:0000255"
FT REPEAT 577..586
FT /note="BNR 6"
FT /evidence="ECO:0000255"
FT REPEAT 616..626
FT /note="BNR 7"
FT /evidence="ECO:0000255"
FT REPEAT 660..671
FT /note="BNR 8"
FT /evidence="ECO:0000255"
FT REPEAT 708..718
FT /note="BNR 9"
FT /evidence="ECO:0000255"
FT DOMAIN 771..841
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 70
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q70DK5"
FT ACT_SITE 480
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q70DK5"
SQ SEQUENCE 842 AA; 92365 MW; 09F04BBE0C9AD179 CRC64;
MVKKFTSKIK AAVFAAVVAA TAIFGPAISS QAVTSVPYKW DNVVIGGGGG FMPGIVFNET
EKDLIYARAD IGGAYRWDPS TETWIPLLDH FQMDEYSYYG VESIATDPVD PNRVYIAAGM
YTNDWLPNMG AILRSTDRGE TWEKTILPFK MGGNMPGRSM GERLAIDPND NRILYLGTRC
GNGLWRSTDY GVTWSKVESF PNPGTYIYDP NFDYTKDIIG VVWVVFDKSS STPGNPTKTI
YVGVADKNES IYRSTDGGVT WKAVPGQPKG LLPHHGVLAS NGMLYITYGD TCGPYDGNGK
GQVWKFNTRT GEWIDITPIP YSSSDNRFCF AGLAVDRQNP DIIMVTSMNA WWPDEYIFRS
TDGGATWKNI WEWGMYPERI LHYEIDISAA PWLDWGTEKQ LPEINPKLGW MIGDIEIDPF
NSDRMMYVTG ATIYGCDNLT DWDRGGKVKI EVKATGIEEC AVLDLVSPPE GAPLVSAVGD
LVGFVHDDLK VGPKKMHVPS YSSGTGIDYA ELVPNFMALV AKADLYDVKK ISFSYDGGRN
WFQPPNEAPN SVGGGSVAVA ADAKSVIWTP ENASPAVTTD NGNSWKVCTN LGMGAVVASD
RVNGKKFYAF YNGKFYISTD GGLTFTDTKA PQLPKSVNKI KAVPGKEGHV WLAAREGGLW
RSTDGGYTFE KLSNVDTAHV VGFGKAAPGQ DYMAIYITGK IDNVLGFFRS DDAGKTWVRI
NDDEHGYGAV DTAITGDPRV YGRVYIATNG RGIVYGEPAS DEPVPTPPQV DKGLVGDLNG
DNRINSTDLT LMKRYILKSI EDLPVEDDLW AADINGDGKI NSTDYTYLKK YLLQAIPELP
KK
