CBHC_EMENI
ID CBHC_EMENI Reviewed; 455 AA.
AC Q5B2E8; C8VH03; Q1HFS7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase C;
DE EC=3.2.1.91;
DE AltName: Full=Beta-glucancellobiohydrolase C;
DE AltName: Full=Exocellobiohydrolase C;
DE AltName: Full=Exoglucanase C;
DE Flags: Precursor;
GN Name=cbhC; ORFNames=AN5282;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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. Active
CC against carboxymethylcellulose, beta-glucan and lichenan.
CC {ECO:0000269|PubMed:16844780}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 57 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at
CC the N-terminus, a linker rich in threonines, and a C-terminal
CC exocellobiohydrolase catalytic module. The genes for catalytic modules
CC and CBMs seem to have evolved separately and have been linked by gene
CC fusion.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF82181.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA62442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490497; ABF50873.1; -; mRNA.
DR EMBL; AACD01000093; EAA62442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001305; CBF82181.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_662886.1; XM_657794.1.
DR AlphaFoldDB; Q5B2E8; -.
DR SMR; Q5B2E8; -.
DR STRING; 162425.CADANIAP00003822; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6C_EMENI; -.
DR EnsemblFungi; EAA62442; EAA62442; AN5282.2.
DR GeneID; 2871574; -.
DR KEGG; ani:AN5282.2; -.
DR VEuPathDB; FungiDB:AN5282; -.
DR eggNOG; ENOG502QWHE; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR InParanoid; Q5B2E8; -.
DR OrthoDB; 957754at2759; -.
DR BRENDA; 3.2.1.91; 517.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IDA:UniProtKB.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..455
FT /note="1,4-beta-D-glucan cellobiohydrolase C"
FT /id="PRO_0000394053"
FT DOMAIN 20..55
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 59..92
FT /note="Thr-rich linker"
FT REGION 66..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..450
FT /note="Catalytic"
FT ACT_SITE 185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 231
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 27..44
FT /evidence="ECO:0000250"
FT DISULFID 38..54
FT /evidence="ECO:0000250"
FT DISULFID 186..245
FT /evidence="ECO:0000250"
FT DISULFID 377..424
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 47624 MW; 32C2655B3E4CCA1F CRC64;
MHYSASGLAL AFLLPAIQAQ QTLYGQCGGS GWTGATSCVA GAACSTLNQW YAQCLPAATT
TSTTLTTTTS SVTTTSNPGS TTTTSSVTVT ATASGNPFSG YQLYVNPYYS SEVQSIAIPS
LTGTLSSLAP AATAAAKVPS FVWLDVAAKV PTMATYLADI RSQNAAGANP PIAGQFVVYD
LPDRDCAALA SNGEFAISDG GVQHYKDYID SIREILVEYS DVHVILVIEP DSLANLVTNL
NVAKCANAQS AYLECTNYAV TQLNLPNVAM YLDAGHAGWL GWPANLQPAA NLYAGVYSDA
GSPAALRGLA TNVANYNAWA IDTCPSYTQG NSVCDEKDYI NALAPLLRAQ GFDAHFITDT
GRNGKQPTGQ QAWGDWCNVI GTGFGARPST NTGDSLLDAF VWVKPGGESD GTSDTSAARY
DAHCGYSDAL QPAPEAGTWF QAYFVQLLQN ANPSF
