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   24-JAN-2024, entry version 95.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 227321.Q5B7R2; -.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; EGL7A_EMENI; -.
DR   GlyCosmos; Q5B7R2; 3 sites, No reported glycans.
DR   EnsemblFungi; CBF82749; CBF82749; ANIA_03418.
DR   GeneID; 2874128; -.
DR   KEGG; ani:AN3418.2; -.
DR   eggNOG; ENOG502RWSR; Eukaryota.
DR   HOGENOM; CLU_020817_0_1_1; -.
DR   InParanoid; Q5B7R2; -.
DR   OMA; ALCPDKK; -.
DR   OrthoDB; 3014058at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
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; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF1; ENDO-BETA-1,4-GLUCANASE CELB; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//