GUXA_CELFA
ID GUXA_CELFA Reviewed; 872 AA.
AC P50401; F4GZL1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Exoglucanase A;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase A;
DE AltName: Full=CBP95;
DE AltName: Full=Exocellobiohydrolase A;
DE Flags: Precursor;
GN Name=cbhA; OrderedLocusNames=Celf_1925;
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX NCBI_TaxID=590998;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RX PubMed=8065260; DOI=10.1111/j.1365-2958.1994.tb01030.x;
RA Meinke A., Gilkes N.R., Kwan E., Kilburn D.G., Warren R.A.J.,
RA Miller R.C. Jr.;
RT "Cellobiohydrolase A (CbhA) from the cellulolytic bacterium Cellulomonas
RT fimi is a beta-1,4-exocellobiohydrolase analogous to Trichoderma reesei CBH
RT II.";
RL Mol. Microbiol. 12:413-422(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 41-58.
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RX PubMed=8458833; DOI=10.1128/jb.175.7.1910-1918.1993;
RA Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.;
RT "Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D
RT (CenD), a family A beta-1,4-glucanase.";
RL J. Bacteriol. 175:1910-1918(1993).
CC -!- FUNCTION: This enzyme hydrolyzes 1,4-beta-D-glucosidic linkages of
CC cellulose. Weak activity against carboxymethylcellulose, bacterial
CC microcrystalline cellulose and barley beta-glucan. Has also weak
CC endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of
CC anomeric configuration.
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 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; L25809; AAC36898.1; -; Unassigned_DNA.
DR EMBL; CP002666; AEE46055.1; -; Genomic_DNA.
DR PIR; S49541; S49541.
DR RefSeq; WP_013771081.1; NC_015514.1.
DR PDB; 7CBD; X-ray; 1.30 A; A=41-483.
DR PDBsum; 7CBD; -.
DR AlphaFoldDB; P50401; -.
DR SMR; P50401; -.
DR STRING; 590998.Celf_1925; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR EnsemblBacteria; AEE46055; AEE46055; Celf_1925.
DR KEGG; cfi:Celf_1925; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_015488_3_0_11; -.
DR OMA; YEWNPNF; -.
DR OrthoDB; 1331351at2; -.
DR SABIO-RK; P50401; -.
DR Proteomes; UP000008460; Chromosome.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:8458833"
FT CHAIN 41..872
FT /note="Exoglucanase A"
FT /id="PRO_0000007904"
FT DOMAIN 484..569
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 579..667
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 677..765
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 763..872
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 41..477
FT /note="Catalytic"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 410
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT DISULFID 140..202
FT /evidence="ECO:0000250"
FT DISULFID 374..428
FT /evidence="ECO:0000250"
FT DISULFID 770..869
FT /evidence="ECO:0000250"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:7CBD"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 200..221
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 241..257
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7CBD"
FT TURN 299..303
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:7CBD"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:7CBD"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:7CBD"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:7CBD"
SQ SEQUENCE 872 AA; 89301 MW; 7883B407F995533B CRC64;
MSTLGKRAGV RRRVRAVATA ATATALVAVP LTTLATSASA APVHVDNPYA GAVQYVNPTW
AASVNAAAGR QSADPALAAK MRTVAGQPTA VWMDRISAIT GNADGNGLKF HLDNAVAQQK
AAGVPLVFNL VIYDLPGRDC FALASNGELP ATDAGLARYK SEYIDPIADL LDNPEYESIR
IAATIEPDSL PNLTTNISEP ACQQAAPYYR QGVKYALDKL HAIPNVYNYI DIGHSGWLGW
DSNAGPSATL FAEVAKSTTA GFASIDGFVS DVANTTPLEE PLLSDSSLTI NNTPIRSSKF
YEWNFDFDEI DYTAHMHRLL VAAGFPSSIG MLVDTSRNGW GGPNRPTSIT ASTDVNAYVD
ANRVDRRVHR GAWCNPLGAG IGRFPEATPS GYAASHLDAF VWIKPPGESD GASTDIPNDQ
GKRFDRMCDP TFVSPKLNNQ LTGATPNAPL AGQWFEEQFV TLVKNAYPVI GGTTPVEDLV
APTVPTGLTA GTTTATSVPL SWTASTDNVA VTGYDVYRGT TLVGTTAATS YTVTGLTPAT
AYSFTVRAKD AAGNVSAASA AAAATTQSGT VTDTTAPSVP AGLTAGTTTT TTVPLSWTAS
TDNAGGSGVA GYEVLRGTTV VGTTTATSYT VTGLTAGTTY SFSVRAKDVA GNTSAASAAV
SATTQTGTVV DTTAPSVPTG LTAGTTTTSS VPLTWTASTD NAGGSGVAGY EVFNGTTRVA
TVTSTSYTVT GLAADTAYSF TVKAKDVAGN VSAASAAVSA RTQAATSGGC TVKYSASSWN
TGFTGTVEVK NNGTAALNGW TLGFSFADGQ KVSQGWSAEW SQSGTAVTAK NAPWNGTLAA
GSSVSIGFNG THNGTNTAPT AFTLNGVACT LG
