ID   MU71A_PENRW             Reviewed;         445 AA.
AC   B6GX22;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Mutanase Pc12g07500 {ECO:0000303|PubMed:24884713};
DE            EC=3.2.1.59 {ECO:0000269|PubMed:24884713};
DE   AltName: Full=Endo-1,3-alpha-glucanase Pc12g07500 {ECO:0000303|PubMed:24884713};
DE   AltName: Full=Glucan endo-1,3-alpha-glucosidas Pc12g07500 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=PCH_Pc12g07500;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24884713; DOI=10.1186/1471-2180-14-114;
RA   Bajaj I., Veiga T., van Dissel D., Pronk J.T., Daran J.M.;
RT   "Functional characterization of a Penicillium chrysogenum mutanase gene
RT   induced upon co-cultivation with Bacillus subtilis.";
RL   BMC Microbiol. 14:114-114(2014).
CC   -!- FUNCTION: Hydrolyzes 1,3-alpha-glucan predominantly into
CC       pentasaccharides. May enhance the efficacy of fungal antibiotics by
CC       degrading bacterial exopolysaccharides. {ECO:0000269|PubMed:24884713}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in
CC         isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59;
CC         Evidence={ECO:0000269|PubMed:24884713};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O13716}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24884713}.
CC   -!- INDUCTION: Expression is induced in response to the presence of
CC       B.subtilis. {ECO:0000269|PubMed:24884713}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 71 family. {ECO:0000305}.
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DR   EMBL; AM920427; CAP80377.1; -; Genomic_DNA.
DR   RefSeq; XP_002557585.1; XM_002557539.1.
DR   AlphaFoldDB; B6GX22; -.
DR   SMR; B6GX22; -.
DR   CAZy; GH71; Glycoside Hydrolase Family 71.
DR   CLAE; MUT71A_PENCH; -.
DR   EnsemblFungi; CAP80377; CAP80377; PCH_Pc12g07500.
DR   GeneID; 8311216; -.
DR   KEGG; pcs:Pc12g07500; -.
DR   VEuPathDB; FungiDB:PCH_Pc12g07500; -.
DR   eggNOG; ENOG502RDR1; Eukaryota.
DR   HOGENOM; CLU_019141_0_0_1; -.
DR   OMA; FAYWNNG; -.
DR   OrthoDB; 405736at2759; -.
DR   BioCyc; PCHR:PC12G07500-MON; -.
DR   BRENDA; 3.2.1.59; 4606.
DR   Proteomes; UP000000724; Contig Pc00c12.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0051118; F:glucan endo-1,3-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11577; GH71; 1.
DR   InterPro; IPR005197; Glyco_hydro_71.
DR   Pfam; PF03659; Glyco_hydro_71; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..445
FT                   /note="Mutanase Pc12g07500"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000408703"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   445 AA;  48546 MW;  B134CE3F956DE79F CRC64;
     MIWKSLFSAL AILTHILPAL TAPALDSELS SQSEDKYVFA HFMVGIVKDY QLEDWKEDMT
     TAQSIGIDAF ALNCASIDSY TPTQLALAYE AAEQVNFKVV ISFDFAYWTN GDTEKITEYM
     KQYAGHPAQM QYKGAAVVST FVGDSFNWDA VKQNTPHPIY AVPNLQDPAE ATTGPAKSAD
     GAFSWLAWPT DGGNSIIPGP MTTVWDDRFV HFLAGKTYMA PVSPWFSTHF NTKNWVFVCE
     NLPTLRWEQM LSLQPDLIEI ISWNDYGESH YIGPYSAHHS DDGSSQWATN MPHDGWRNLF
     KPYIAAYKSG AKTPTVEADE VVYWYRPTPK GVVCTGDTLS APMGADMLSD SIFVATMLTS
     PGTLTVQSGN NAPVDIEVPA GIVTSNVTMG VGAQSFKVAR DGQTILSGQG GLDVKDSCVH
     YNFNVYVGST KGGDGSNTTG ARGSM