ID   XYNX_ACETH              Reviewed;        1087 AA.
AC   P38535;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Exoglucanase XynX;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase;
DE   AltName: Full=Exocellobiohydrolase;
DE   Flags: Precursor;
GN   Name=xynX;
OS   Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS   thermocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pack M.Y., Jung K.H.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC         and cellotetraose, releasing cellobiose from the non-reducing ends of
CC         the chains.; EC=3.2.1.91;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; M67438; AAA23227.1; -; Genomic_DNA.
DR   PIR; S41797; S41797.
DR   AlphaFoldDB; P38535; -.
DR   SMR; P38535; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00005; CBM9_like_1; 1.
DR   Gene3D; 2.60.40.1190; -; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF06452; CBM9_1; 2.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00395; SLH; 3.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49344; CBD9-like; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS51272; SLH; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..1087
FT                   /note="Exoglucanase XynX"
FT                   /id="PRO_0000007982"
FT   DOMAIN          37..188
FT                   /note="CBM-cenC"
FT   DOMAIN          204..527
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   DOMAIN          903..966
FT                   /note="SLH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   DOMAIN          967..1025
FT                   /note="SLH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   DOMAIN          1028..1087
FT                   /note="SLH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   ACT_SITE        347
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        452
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   1087 AA;  120358 MW;  88077FC27AC83F51 CRC64;
     MKNNLSKFVS IFTAFIMIFG TSLFFPHVSA FADDNNANLV SNGDFESGTI DGWIKQGNPT
     LAATTEEAIG QYSMKVAGRT QTYEGPAYSF LGKMQKGQSY NVSLKVRLVS GQNSSNPLIT
     VTMFREDDNG KHYDTIVWQK QVSEDSWTTV NGTYTLDYTG TLKTLYMYVE SPDPTLEYYI
     DDVVVTPQNP IQVGEISNNQ ITIQNDIPDL SSVFKDYFPI GVAVDPSRLN DTDPHAQLTA
     KHFNMLVAEN AMKPESLQPT EGNFTFDNAD RIVDYAIAHN MKMRGHTLLW HNQVPDWFFQ
     DPSDPTKPAS RDLLLQRLKT HITTVLDHFK TKYGAQNPII GWDVVNEVLD DNGSLRNSKW
     LQIIGPDYIE KAFEYAHEAD PSMKLFINDY NIENNGVKTQ AMYDLVKKLK SEGVPISGIG
     MQMHININSN IDNIKASIEK LASLGVEIQV TELDMNMNGN VSNEALLKQA RLYKQLFDLF
     KAEKQYITAV VFWGVSDDVT WLSKPNAPLL FDSKLQAKPA YWAIADPSKA IPDIQSAKAL
     EGSPTIGANV DSSWKLVKPL YANTYVEGTV GATATVKSMW DTKNLYLLVQ VSDNTPSSND
     GIEIFVDKND NKSTSYETDD EHYTIKSDGT GSSDITKYVT SNADGYIVQL AIPIEDISPT
     LNDKIGLDVR LNDDKGSGSI DTVTVWNDYT NSQDTNTSYF GDIVLSKPAQ VATAIYGTPV
     IDGKIDDIWN KVDAITTNTW VLGSDGATAT AKMMWDDKYL YVLADVTDSN LNKSSVNPYE
     QDSVEVFVDQ NNDKTSYYES DDGQYRVNYD NEQSFGGSTN SNGFKSATSL TQSGYIVEEA
     IPWTSITLLN GTIIGFDLQV NDADENGKRT GIVTWCDPSG NSWQDTSGFG NLLLTGKPSG
     VLKKSVTFND IKDNWAKDVI EVLASRHIVE GMTDTQYEPS KTVTRAEFTA MILKLLNIKE
     EAYNGEFSDV KNGDWYANAI EAAYKAGIIE GDGKNMRPND SITREEMTSI AMRAYEMLTS
     YKEENIGATS FNDDKSISDW AKNVVANAAK LGIINGEPSN VFAPKGIATR AEAAAIIYGL
     LEKSNNL
//