ID   MANA_ASPAC              Reviewed;         377 AA.
AC   Q00012;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=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;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=KSM 510;
RX   PubMed=7987261;
RA   Christgau S., Kauppinen S., Vind J., Kofod L.V., Dalboge H.;
RT   "Expression cloning, purification and characterization of a beta-1,4-
RT   mannanase from Aspergillus aculeatus.";
RL   Biochem. Mol. Biol. Int. 33:917-925(1994).
CC   -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC       seed galactomannans and wood galactoglucomannans.
CC       {ECO:0000269|PubMed:7987261}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:7987261};
CC       Temperature dependence:
CC         Optimum temperature is between 60 and 70 degrees Celsius.
CC         {ECO:0000269|PubMed:7987261};
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; L35487; AAA67426.1; -; mRNA.
DR   AlphaFoldDB; Q00012; -.
DR   SMR; Q00012; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; MAN5A_ASPAC; -.
DR   VEuPathDB; FungiDB:ASPACDRAFT_32506; -.
DR   BRENDA; 3.2.1.78; 488.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..377
FT                   /note="Mannan endo-1,4-beta-mannosidase A"
FT                   /id="PRO_5000142576"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        306
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   377 AA;  41082 MW;  10E6477555BE3CA2 CRC64;
     MKLSHMLLSL ASLGVATALP RTPNHNAATT AFPSTSGLHF TIDGKTGYFA GTNSYWIGFL
     TNNDDVDLVM SQLAASDLKI LRVWGFNDVN TKPTDGTVWY QLHANGTSTI NTGADGLQRL
     DYVVTSAEKY GVKLIINFVN EWTDYGGMQA YVTAYGAAAQ TDFYTNTAIQ AAYKNYIKAV
     VSRYSSSAAI FAWELANEPR CQGCDTSVLY NWISDTSKYI KSLDSKHLVT IGDEGFGLDV
     DSDGSYPYTY GEGLNFTKNL GISTIDFGTL HLYPDSWGTS YDWGNGWITA HAAACKAVGK
     PCLLEEYGVT SNHCAVESPW QQTAGNATGI SGDLYWQYGT TFSWGQSPND GNTFYYNTSD
     FTCLVTDHVA AINAQSK