ID   MANA_ASPFN              Reviewed;         386 AA.
AC   B8NVK8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 61.
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=AFLA_116950;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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=EED45466.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; EQ963485; EED45466.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002384402.1; XM_002384361.1.
DR   AlphaFoldDB; B8NVK8; -.
DR   SMR; B8NVK8; -.
DR   STRING; 5059.CADAFLAP00012267; -.
DR   EnsemblFungi; EED45466; EED45466; AFLA_116950.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   Proteomes; UP000001875; 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; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..386
FT                   /note="Probable mannan endo-1,4-beta-mannosidase A"
FT                   /id="PRO_0000393702"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  42008 MW;  F30ED415E9A34993 CRC64;
     MKLNPSLLTA AGLVSAQLAS ALPQASSSTV SPSPSPSATP GSFVTTSGLN FVIDGKTGYF
     AGSNSYWIGF QKNNDDVDLV FSHLQESGLK ILRVWGFNDV NQKPTDGSVY YHLLADGTAT
     VNEGEDGLQR LDYVVSSAEK HGIKLIINFV NFWDDYGGIN AYVKAFGGSK EDFYTNDAMQ
     AAYRAYIKAV ISRYSDSTAI FAWELANEPR CQGCETTVLY NWIESTSQYI KSLDSKHLVC
     IGDEGFGLDT GSDGSYPYQY SEGSDFAKNL AIPTIDFGTF HLYPSSWGTT NDWGNGWVTS
     HGAACKEAGK PCLFEEYGVT SDHCAVEKPW QNTALNTTAI SGDLYWQYGD QLSGGPSPDD
     GNTFYYGTDD FKCLVTDHIA AINSRN