GUX1_PHACH
ID GUX1_PHACH Reviewed; 516 AA.
AC P13860;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Exoglucanase 1;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Exocellobiohydrolase I;
DE AltName: Full=Exoglucanase I;
DE Flags: Precursor;
GN Name=CBH1;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750;
RX PubMed=3246351; DOI=10.1016/0378-1119(88)90174-6;
RA Sims P.F.G., James C., Broda P.;
RT "The identification, molecular cloning and characterisation of a gene from
RT Phanerochaete chrysosporium that shows strong homology to the exo-
RT cellobiohydrolase I gene from Trichoderma reesei.";
RL Gene 74:411-422(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750;
RX PubMed=8057846; DOI=10.1111/j.1365-2958.1994.tb01010.x;
RA Sims P.F.G., Soares-Felipe M.S., Wang Q., Gent M.E., Tempelaars C.,
RA Broda P.;
RT "Differential expression of multiple exo-cellobiohydrolase I-like genes in
RT the lignin-degrading fungus Phanerochaete chrysosporium.";
RL Mol. Microbiol. 12:209-216(1994).
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; M22220; AAB46373.1; -; Genomic_DNA.
DR EMBL; Z22528; CAA80253.1; -; mRNA.
DR PIR; JS0083; JS0083.
DR PIR; S33164; S33164.
DR AlphaFoldDB; P13860; -.
DR SMR; P13860; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; CBH7A_PHACH; -.
DR VEuPathDB; FungiDB:AGR57_12414; -.
DR BioCyc; MetaCyc:MON-17639; -.
DR BRENDA; 3.2.1.176; 1380.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..516
FT /note="Exoglucanase 1"
FT /id="PRO_0000007924"
FT DOMAIN 480..516
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION ?..449
FT /note="Catalytic"
FT REGION 450..480
FT /note="Linker"
FT REGION 451..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 488..505
FT /evidence="ECO:0000250"
FT DISULFID 499..515
FT /evidence="ECO:0000250"
FT CONFLICT 27..28
FT /note="RS -> EN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..31
FT /note="PA -> RT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 54858 MW; 1C7C3D338ECE1B72 CRC64;
MFRTATLLAF TMAAMVFGQQ VGTNTARSHP ALTSQKCTKS GGCSNLNTKI VLDANWRWLH
STSGYTNCYT GNQWDATLCP DGKTCAANCA LDGADYTGTY GITASGSSLK LQFVTGSNVG
SRVYLMADDT HYQMFQLLNQ EFTFDVDMSN LPCGLNGALY LSAMDADGGM AKYPTNKAGA
KYGTGYCDSQ CPRDIKFING EANVEGWNAT SANAGTGNYG TCCTEMDIWE ANNDAAAYTP
HPCTTNAQTR CSGSDCTRDT GLCDADGCDF NSFRMGDQTF LGKGLTVDTS KPFTVVTQFI
TNDGTSAGTL TEIRRLYVQN GKVIQNSSVK IPGIDPVNSI TDNFCSQQKT AFGDTNYFAQ
HGGLKQVGEA LRTGMVLALS IWDDYAANML WLDSNYPTNK DPSTPGVARG TCATTSGVPA
QIEAQSPNAY VVFSNIKFGD LNTTYTGTVS SSSVSSSHSS TSTSSSHSSS STPPTQPTGV
TVPQWGQCGG IGYTGSTTCA SPYTCHVLNP YYSQCY
