ID   MANA1_ASPTN             Reviewed;         388 AA.
AC   Q0CCD0;
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 A-1;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-beta-1,4-mannanase A-1;
DE   Flags: Precursor;
GN   Name=manA-1; Synonyms=man1-1; ORFNames=ATEG_08654;
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; CH476606; EAU30786.1; -; Genomic_DNA.
DR   RefSeq; XP_001217240.1; XM_001217239.1.
DR   AlphaFoldDB; Q0CCD0; -.
DR   SMR; Q0CCD0; -.
DR   STRING; 341663.Q0CCD0; -.
DR   EnsemblFungi; EAU30786; EAU30786; ATEG_08654.
DR   GeneID; 4323372; -.
DR   VEuPathDB; FungiDB:ATEG_08654; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_4_1_1; -.
DR   OMA; EAPWQKT; -.
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..388
FT                   /note="Probable mannan endo-1,4-beta-mannosidase A-1"
FT                   /id="PRO_0000393703"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        315
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   388 AA;  41993 MW;  FE35377CB387E076 CRC64;
     MKLSPLMALA GLASAQLALA LPQATPSASA TPSPTPGDGS FASTNGLQFV IDGETGYFAG
     SNSYWIGFLT NNADVDLVFT HMKEAGLRIL RVWGFNDVNE KPADGTVWFQ MHADGQSTIN
     TGADGLQRLD YVVQSAEKHG IKLIVNFVNY WDDYGGMNAY VQAYGGSDNT DFYASKDMQA
     AYRAYIKAVV SRYLDSPAIF AWELANEPRC QGCAPSVLHD WIDSTSQYIK SLDSKHMTCI
     GDEGFGLDIG SDGSYPYGYS EGGNFTMSLA LPTIDFGTFH LYPSSWGTNN DWGNGWVASH
     GAACKAAGKP CLFEEYGVTS DHCAVEKPWQ MTALNTTGIA ADLYWQYGDQ LSSGQSPNDG
     NTIYYGTDEF TCLVTDHIAS IGSRATRK