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MANA2_ASPTN
ID   MANA2_ASPTN             Reviewed;         396 AA.
AC   Q0CUG5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable mannan endo-1,4-beta-mannosidase A-2;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-beta-1,4-mannanase A-2;
DE   Flags: Precursor;
GN   Name=manA-2; Synonyms=man1-2; ORFNames=ATEG_02669;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU37631.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH476596; EAU37631.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001211847.1; XM_001211847.1.
DR   AlphaFoldDB; Q0CUG5; -.
DR   SMR; Q0CUG5; -.
DR   STRING; 341663.Q0CUG5; -.
DR   EnsemblFungi; EAU37631; EAU37631; ATEG_02669.
DR   GeneID; 4317245; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   OMA; TQWITDH; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..396
FT                   /note="Probable mannan endo-1,4-beta-mannosidase A-2"
FT                   /id="PRO_0000393704"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   396 AA;  43756 MW;  D326B27A4DADC65C CRC64;
     MKVPRLLLAL GGLASIHIAS ALPQGAVERD MHATSAVVHG GNVKTKFPST TGLKFTIDGE
     TGYFAGSNSY WIGFLTNNAD VDLVFQHMKE SGLKILRVWG FNDVNTKPAT GTVWYQLHAN
     GTSTINTGPD GLQRLDYVVH SAERHGIKLI INFVNNWNDY GGINSYLQAY GGASNEDFYN
     SEPMQKAYRA YIKEVVSRYI DSPAVFAWEL ANEPRCKGCD TSVLHSWIEK TSRYIKSLDK
     KHMVTTGEEG FGLDLMSDGS YPFTYVEGGN FTDTLSIPTI DFGTFHLYPS SWGTTNDWGN
     LWVEAHGAAC KAAGKPRLFE EYGVTADHCA LEKPWQTTAL KTKGVSGDLY WQYGDTLSTG
     PSPDDGNTFY YGTDEFDCLV SDHVAAIDEM EKHGRH
 
 
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