MANF_ASPOR
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 03-AUG-2022, entry version 84.
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 CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblFungi; BAE64232; BAE64232; AO090038000444.
DR VEuPathDB; FungiDB:AO090038000444; -.
DR OMA; LFWQYGQ; -.
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 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; PTHR31451; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 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
