ID   MANC_ASPTN              Reviewed;         406 AA.
AC   Q0C8J3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable mannan endo-1,4-beta-mannosidase C;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-beta-1,4-mannanase C;
DE   Flags: Precursor;
GN   Name=manC; ORFNames=ATEG_09991;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC       seed galactomannans and wood galactoglucomannans. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC         mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; CH476609; EAU29440.1; -; Genomic_DNA.
DR   RefSeq; XP_001209293.1; XM_001209293.1.
DR   AlphaFoldDB; Q0C8J3; -.
DR   SMR; Q0C8J3; -.
DR   STRING; 341663.Q0C8J3; -.
DR   EnsemblFungi; EAU29440; EAU29440; ATEG_09991.
DR   GeneID; 4319511; -.
DR   VEuPathDB; FungiDB:ATEG_09991; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_4_0_1; -.
DR   OMA; QRWMEEM; -.
DR   OrthoDB; 1003648at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045053; MAN-like.
DR   PANTHER; PTHR31451; PTHR31451; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..406
FT                   /note="Probable mannan endo-1,4-beta-mannosidase C"
FT                   /id="PRO_0000393709"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   406 AA;  45768 MW;  2D17F17F4806AC93 CRC64;
     MLINFEKVLS LALLAGSVSG RKHVPRGFVT TSGMKFQLDG KDFYFAGSNA YYFPFNDNQT
     DVELGLAAAK QAGLTVFRTW GFNDKNATYI EGGLPAYGGE GAGTTEVVFQ RWANGTSTID
     LEPFDKVVNA AKNTGMKLVV ALTNNWADYG GMDVYTINLG GQYHDDFYRL PAIKKAYKRY
     VKEMVTRYRD SPAIMAWELA NEPRCGADGV RNLPRSADGC NPEVLTAWID EMSTYIKKLD
     PHHLVTWGGE GGFNIESDDW AYNGADGGDF DNELALPNID FGVFHSYPDW WSKTVSWTNQ
     WIRDHAAAMR TGRKPVVHEE YGWLTPEARL EYLGTVSNIT RLEAVGGWQQ ISVSEKMSDM
     YWQYGYSGYS YGRNHNDGFT IYLDDPEAKE LVYKHAKEVK KLNRRH