ID   MANA_ASPCL              Reviewed;         360 AA.
AC   A1CGC6;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable mannan endo-1,4-beta-mannosidase A;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-beta-1,4-mannanase A;
DE   Flags: Precursor;
GN   Name=manA; Synonyms=man1; ORFNames=ACLA_066420;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027053; EAW11006.1; -; Genomic_DNA.
DR   RefSeq; XP_001272432.1; XM_001272431.1.
DR   AlphaFoldDB; A1CGC6; -.
DR   SMR; A1CGC6; -.
DR   STRING; 5057.CADACLAP00006059; -.
DR   EnsemblFungi; EAW11006; EAW11006; ACLA_066420.
DR   GeneID; 4704555; -.
DR   KEGG; act:ACLA_066420; -.
DR   VEuPathDB; FungiDB:ACLA_066420; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_4_1_1; -.
DR   OMA; EAPWQKT; -.
DR   OrthoDB; 1003648at2759; -.
DR   Proteomes; UP000006701; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..360
FT                   /note="Probable mannan endo-1,4-beta-mannosidase A"
FT                   /id="PRO_0000393701"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   360 AA;  39457 MW;  B25067154F8DBF70 CRC64;
     MKLSQILTFA SLLSGALAAP GKPHGKPGFA STSGLQFSID GQTGYFAGSN SYWIGFLTNK
     ADVDIGFNDV NTVPGEGTVY YQLHANGKST INTGANGLQR MDYVVKSAEK HGIKLIINFV
     NNWDDYGGMN AYVKGYGAAD HNDFYSNAKI QKAYRQYIRA VVSRYTKSDA VFAWELANEP
     RCKGCDTDVL YDWIKSTSEY IKSLDAKHMV CIGDEGFGLE TLSDGSYPFT YVEGSDFARN
     LAIPTIDFGT FHLYPDSWGT SHEWGNLWTQ AHGAACQAAG KPCLFEEYGV TSDHCALETP
     WQKTSLNTTG VSADLYWQYG DTLSSGPSPN DGHTVYYGTD DFKCMVTDHV AAIKAKQGWV