MANF_ASPFU
ID MANF_ASPFU Reviewed; 438 AA.
AC Q4WBS1; B5LZ77; B5LZ78;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=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=AFUA_8G07030;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-438, PROTEIN SEQUENCE OF 18-29;
RP 113-133 AND 325-347, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=IMI 385708;
RX PubMed=15541293; DOI=10.1016/j.bbagen.2004.06.022;
RA Puchart V., Vrsanska M., Svoboda P., Pohl J., Ogel Z.B., Biely P.;
RT "Purification and characterization of two forms of endo-beta-1,4-mannanase
RT from a thermotolerant fungus, Aspergillus fumigatus IMI 385708 (formerly
RT Thermomyces lanuginosus IMI 158749).";
RL Biochim. Biophys. Acta 1674:239-250(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-438, FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=IMI 385708;
RX PubMed=19205049; DOI=10.1002/btpr.104;
RA Duruksu G., Ozturk B., Biely P., Bakir U., Ogel Z.B.;
RT "Cloning, expression and characterization of endo-beta-1,4-mannanase from
RT Aspergillus fumigatus in Aspergillus sojae and Pichia pastoris.";
RL Biotechnol. Prog. 25:271-276(2009).
CC -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC seed galactomannans and wood galactoglucomannans.
CC {ECO:0000269|PubMed:15541293, ECO:0000269|PubMed:19205049}.
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 Kinetic parameters:
CC KM=3.07 mM for locust bean galactomannan
CC {ECO:0000269|PubMed:15541293, ECO:0000269|PubMed:19205049};
CC Vmax=1935 umol/min/mg enzyme {ECO:0000269|PubMed:15541293,
CC ECO:0000269|PubMed:19205049};
CC pH dependence:
CC Optimum pH is 4.0 to 5.0. {ECO:0000269|PubMed:15541293,
CC ECO:0000269|PubMed:19205049};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Stable up to 55 degrees
CC Celsius. {ECO:0000269|PubMed:15541293, ECO:0000269|PubMed:19205049};
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=EAL85463.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAHF01000013; EAL85463.1; ALT_INIT; Genomic_DNA.
DR EMBL; EU925594; ACH58410.1; -; Genomic_DNA.
DR EMBL; EU925595; ACH58411.1; -; mRNA.
DR RefSeq; XP_747501.1; XM_742408.1.
DR AlphaFoldDB; Q4WBS1; -.
DR SMR; Q4WBS1; -.
DR STRING; 746128.CADAFUBP00007866; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR GeneID; 3504904; -.
DR KEGG; afm:AFUA_8G07030; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_4_1_1; -.
DR InParanoid; Q4WBS1; -.
DR OrthoDB; 1003648at2759; -.
DR BRENDA; 3.2.1.78; 508.
DR Proteomes; UP000002530; Chromosome 8.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:15541293"
FT CHAIN 18..438
FT /note="Mannan endo-1,4-beta-mannosidase F"
FT /id="PRO_0000393715"
FT DOMAIN 19..54
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 60..96
FT /note="Ser-rich linker"
FT REGION 61..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..438
FT /note="Catalytic"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14..17
FT /note="GAVA -> IYGS (in Ref. 2; ACH58410)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> S (in Ref. 3; ACH58411)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..236
FT /note="KIQ -> QIP (in Ref. 3; ACH58411)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="P -> L (in Ref. 3; ACH58411)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="T -> A (in Ref. 3; ACH58411)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="L -> P (in Ref. 3; ACH58411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 47327 MW; 8E55123506BD7E24 CRC64;
MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY SQCQPATTTS
TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA DGLKFNIDGE TKYFAGTNAY
WLPFLTNDAD VDSVMDNLQK AGLKILRTWG FNDVNSKPSS GTVYFQLHDP STGTTTINTG
ADGLQRLDYV VSAAEKRGIK LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ
AYIKAVVSRY RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE
GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW GNGWVTSHAK
VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL FWQYGQTLST GPSPNDHFTI
YYGTSDWQCG VADHLSTL
