ID   MANF_ASPOR              Reviewed;         463 AA.
AC   Q2U2I3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Probable mannan endo-1,4-beta-mannosidase F;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-beta-1,4-mannanase F;
DE   Flags: Precursor;
GN   Name=manF; ORFNames=AO090038000444;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at
CC       the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-
CC       mannanase catalytic module. The genes for catalytic modules and CBMs
CC       seem to have evolved separately and have been linked by gene fusion.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE64232.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007169; BAE64232.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001825365.2; XM_001825313.2.
DR   AlphaFoldDB; Q2U2I3; -.
DR   SMR; Q2U2I3; -.
DR   STRING; 510516.Q2U2I3; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GlyCosmos; Q2U2I3; 1 site, No reported glycans.
DR   EnsemblFungi; BAE64232; BAE64232; AO090038000444.
DR   VEuPathDB; FungiDB:AO090038000444; -.
DR   OMA; LFWQYGQ; -.
DR   OrthoDB; 2717493at2759; -.
DR   Proteomes; UP000006564; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045053; MAN-like.
DR   PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR   PANTHER; PTHR31451:SF60; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 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..463
FT                   /note="Probable mannan endo-1,4-beta-mannosidase F"
FT                   /id="PRO_0000393716"
FT   DOMAIN          19..54
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          57..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..118
FT                   /note="Ser-rich linker"
FT   REGION          93..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..463
FT                   /note="Catalytic"
FT   COMPBIAS        93..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        286
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        395
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   463 AA;  49992 MW;  8926BA2E033A383B CRC64;
     MRSLSSIALL SVVGAASAQA GPWAQCGGKS FSGSSECASG WKCQELNEWF SQCVPGAEST
     TPTVSSTPTP TDAPSVSITA SVTTGINKSI SVSSASKSTP LPSSSSASPS PRPTGSGSFA
     KADGLQFSID GETKYFAGTN AYWLPFQMND ADIDSVFDHL EQAGLKILRV WGFNDVNTAP
     SPGTVYFQLH DKEKGTSTIN TGKDGLQRLD YVVAAAEKHG VKLIIPFVNS WDDYGGYNAY
     VKAYGGSKTE WFTNEKIQSV YQAYIKAVVS RYRDSPAIFA WELGNEPRCS GCSTDVIHGW
     ATKISAYIKS LDPNHMVALG DEGMGLTIGS DQSYPYGTSE GNDFEKNLAI PDIDFGTLHL
     YTTDWGIKDN AWGNGWVENH AKACKAAGKP CLFEEYGMKG NHCTDELKWQ KTSLSSGTAA
     DLIWQYGQQL STGESPKDAY SIFYGTDEWK CAVMDHMENV NKN
//