CELB_EMENI
ID CELB_EMENI Reviewed; 430 AA.
AC Q5B7R2; C8VHK3; Q8NK01;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Endo-beta-1,4-glucanase celB;
DE Short=Endoglucanase celB;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethylcellulase celB;
DE AltName: Full=Cellulase B;
DE Flags: Precursor;
GN Name=celB; Synonyms=eglB, eglC; ORFNames=AN3418;
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 [GENOMIC DNA].
RX PubMed=12409103; DOI=10.1016/s1087-1845(02)00504-2;
RA Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M.;
RT "Regulation by carbon and nitrogen sources of a family of cellulases in
RT Aspergillus nidulans.";
RL Fungal Genet. Biol. 37:190-196(2002).
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).
RN [4]
RP 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).
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates.
CC {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; AF420021; AAM54071.1; -; Genomic_DNA.
DR EMBL; AACD01000055; EAA63386.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF82749.1; -; Genomic_DNA.
DR RefSeq; XP_661022.1; XM_655930.1.
DR AlphaFoldDB; Q5B7R2; -.
DR SMR; Q5B7R2; -.
DR STRING; 162425.CADANIAP00009621; -.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; EGL7A_EMENI; -.
DR EnsemblFungi; CBF82749; CBF82749; ANIA_03418.
DR EnsemblFungi; EAA63386; EAA63386; AN3418.2.
DR GeneID; 2874128; -.
DR KEGG; ani:AN3418.2; -.
DR eggNOG; ENOG502RWSR; Eukaryota.
DR HOGENOM; CLU_020817_0_1_1; -.
DR InParanoid; Q5B7R2; -.
DR OMA; NEMDIFE; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
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; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..430
FT /note="Endo-beta-1,4-glucanase celB"
FT /id="PRO_0000395159"
FT ACT_SITE 216
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 45
FT /note="S -> Y (in Ref. 1; AAM54071)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="P -> R (in Ref. 1; AAM54071)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> Y (in Ref. 1; AAM54071)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="N -> Y (in Ref. 1; AAM54071)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="E -> D (in Ref. 1; AAM54071)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="C -> W (in Ref. 1; AAM54071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 45929 MW; 4807FA907F18749E CRC64;
MALLLSLSLL ATTISAQQIG TPEIRPRLTT YHCTSANGCT EQNTSVVLDA ATHPIHDASN
PSVSCTTSNG LNPALCPDKQ TCADNCVIDG ITDYAAHGVE THGSRLTLTQ YRNVNGALSS
VSPRVYLVDE SDPDEQEYRA LSLLAQEFTF TVNVSALPCG MNGALYLSEM SPSGGRSALN
PAGASYGTGY CDAQCYVNPW INGEGNINGY GACCNEMDIW EANSRSTGFT PHACLYEPEE
TEGRGVYECA SEDECDSAGE NDGICDKWGC GFNPYALGNT EYYGRGQGFE VDTKEPFTVV
TQFLTDDGTS TGALTEIRRL YIQNGQVIEN AVVSSGADSL TDSLCASTAS WFDSYGGMEG
MGRALGRGMV LAMSIWNDAG GYMQWLDGGD AGPCNATEGA PEFIEEHTPW TRVVFEDLKW
GDIGSTFQAS
