MANA_HYPJR
ID MANA_HYPJR Reviewed; 437 AA.
AC Q99036; A0A024SIJ3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase A;
DE EC=3.2.1.78 {ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3, ECO:0000269|Ref.4};
DE AltName: Full=Beta-mannanase 5A;
DE Short=Man5A {ECO:0000303|PubMed:12523968};
DE AltName: Full=Beta-mannanase I/II {ECO:0000303|PubMed:8529653};
DE Short=BMANI;
DE Short=BMANII;
DE AltName: Full=Endo-beta-1,4-mannanase A;
DE Flags: Precursor;
GN Name=man1 {ECO:0000303|PubMed:7793911};
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE OF 28-42.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=7793911; DOI=10.1128/aem.61.3.1090-1097.1995;
RA Staalbrand H., Saloheimo A., Vehmaanperae J., Henrissat B., Penttilae M.;
RT "Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei
RT beta-mannanase gene containing a cellulose binding domain.";
RL Appl. Environ. Microbiol. 61:1090-1097(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1007/BF00166849;
RA Arisan-Atac I., Hodits R., Kristufek D., Kubicek C.P.;
RT "Purification, and characterization of a beta-mannanase of Trichoderma
RT reesei C-30.";
RL Appl. Microbiol. Biotechnol. 39:58-62(1993).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1016/0168-1656(93)90055-R;
RA Staalbrand H.;
RT "Purification and characterization of two beta-mannanases from Trichoderma
RT reesei.";
RL J. Biotechnol. 29:229-242(1993).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8529653; DOI=10.1111/j.1432-1033.1995.278_c.x;
RA Harjunpaeae V., Teleman A., Siika-Aho M., Drakenberg T.;
RT "Kinetic and stereochemical studies of manno-oligosaccharide hydrolysis
RT catalysed by beta-mannanases from Trichoderma reesei.";
RL Eur. J. Biochem. 234:278-283(1995).
RN [6]
RP DOMAIN.
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX PubMed=12523968; DOI=10.1016/s0168-1656(02)00290-0;
RA Haegglund P., Eriksson T., Collen A., Nerinckx W., Claeyssens M.,
RA Staalbrand H.;
RT "A cellulose-binding module of the Trichoderma reesei beta-mannanase Man5A
RT increases the mannan-hydrolysis of complex substrates.";
RL J. Biotechnol. 101:37-48(2003).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-198.
RX DOI=10.3109/10242422.2012.674726;
RA Rosengren A., Haegglund P., Anderson L., Pavon-Orozco P.,
RA Peterson-Wulff R., Nerinckx W., Staalbrand H.;
RT "The role of subsite +2 of the Trichoderma reesei beta-mannanase TrMan5A in
RT hydrolysis and transglycosylation.";
RL Biocatal. Biotransformation 30:338-352(2012).
RN [8]
RP FUNCTION.
RX PubMed=24950755; DOI=10.1007/s00253-014-5871-8;
RA Rosengren A., Reddy S.K., Sjoeberg J.S., Aurelius O., Logan D.T.,
RA Kolenova K., Staalbrand H.;
RT "An Aspergillus nidulans beta-mannanase with high transglycosylation
RT capacity revealed through comparative studies within glycosidase family
RT 5.";
RL Appl. Microbiol. Biotechnol. 98:10091-10104(2014).
RN [9] {ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP, ECO:0007744|PDB:1QNQ}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 28-371 IN COMPLEX WITH
RP MANNOBIOSE, GLYCOSYLATION AT ASN-157; ASN-184; ASN-277 AND ASN-355,
RP DISULFIDE BONDS, AND ACTIVE SITE.
RX PubMed=10666621; DOI=10.1107/s0907444999013943;
RA Sabini E., Schubert H., Murshudov G., Wilson K.S., Siika-Aho M.,
RA Penttila M.;
RT "The three-dimensional structure of a Trichoderma reesei beta-mannanase
RT from glycoside hydrolase family 5.";
RL Acta Crystallogr. D 56:3-13(2000).
CC -!- FUNCTION: Endo-1,4-mannanase that catalyzes the random hydrolysis of
CC (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a
CC crucial enzyme for depolymerization of seed galactomannans and wood
CC galactoglucomannans. Active against locust bean gum and ivory nut
CC mannan, releasing mainly tri- and disaccharides (PubMed:7793911, Ref.3,
CC Ref.4, PubMed:8529653). Also has transglycosylation activity.
CC Transglycosylation of two mannotrioses into a mannohexaose is the major
CC transglycosylation route (PubMed:8529653, Ref.7, PubMed:24950755).
CC {ECO:0000269|PubMed:24950755, ECO:0000269|PubMed:7793911,
CC ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3, ECO:0000269|Ref.4,
CC ECO:0000269|Ref.7}.
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 Evidence={ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3,
CC ECO:0000269|Ref.4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0015 mg/ml for locust bean gum mannan {ECO:0000269|Ref.3};
CC KM=0.6 mg/ml for locust bean gum mannan {ECO:0000269|Ref.7};
CC KM=0.25 mM for 4-methylumbelliferyl-mannotrioside
CC {ECO:0000269|Ref.7};
CC KM=0.31 mM for mannotetraose {ECO:0000269|Ref.7};
CC KM=0.08 mM for mannopentaose {ECO:0000269|Ref.7};
CC KM=0.05 mM for mannohexaose {ECO:0000269|Ref.7};
CC pH dependence:
CC Optimum pH is 5.0. Stable from pH 2.5 to 7.0. {ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius. {ECO:0000269|Ref.3};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:B2B3C0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
CC -!- DOMAIN: The enzyme consists of two functional domains, a catalytic core
CC joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-,
CC and proline-rich, highly glycosylated linker sequence (Probable). The
CC CBM binds to cellulose but not to mannan, and increases the mannan-
CC hydrolysis of complex substrates (PubMed:12523968).
CC {ECO:0000269|PubMed:12523968, ECO:0000305|PubMed:7793911}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; L25310; AAA34208.1; -; mRNA.
DR EMBL; KI911141; ETS04541.1; -; Genomic_DNA.
DR PDB; 1QNO; X-ray; 2.00 A; A=28-371.
DR PDB; 1QNP; X-ray; 1.50 A; A=28-371.
DR PDB; 1QNQ; X-ray; 1.65 A; A=28-371.
DR PDB; 1QNR; X-ray; 1.40 A; A=28-371.
DR PDB; 1QNS; X-ray; 1.50 A; A=28-371.
DR PDBsum; 1QNO; -.
DR PDBsum; 1QNP; -.
DR PDBsum; 1QNQ; -.
DR PDBsum; 1QNR; -.
DR PDBsum; 1QNS; -.
DR AlphaFoldDB; Q99036; -.
DR SMR; Q99036; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR iPTMnet; Q99036; -.
DR EnsemblFungi; ETS04541; ETS04541; M419DRAFT_122377.
DR KEGG; trr:M419DRAFT_122377; -.
DR OrthoDB; 1003648at2759; -.
DR BRENDA; 3.2.1.78; 6451.
DR EvolutionaryTrace; Q99036; -.
DR Proteomes; UP000024376; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0048030; F:disaccharide binding; IDA:UniProtKB.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0046355; P:mannan catabolic process; IDA:UniProtKB.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:7793911"
FT /id="PRO_0000441278"
FT CHAIN 28..437
FT /note="Mannan endo-1,4-beta-mannosidase A"
FT /id="PRO_5004322683"
FT DOMAIN 400..435
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 28..376
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:7793911"
FT REGION 372..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..399
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:7793911"
FT COMPBIAS 372..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:10666621"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:10666621"
FT BINDING 196..198
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNR"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNR"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNR"
FT SITE 198
FT /note="Important for transglycosylation activity"
FT /evidence="ECO:0000269|Ref.7"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT DISULFID 53..56
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT DISULFID 199..202
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT DISULFID 292..299
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT DISULFID 311..361
FT /evidence="ECO:0000269|PubMed:10666621,
FT ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP,
FT ECO:0007744|PDB:1QNQ"
FT MUTAGEN 198
FT /note="R->K: Shows an altered product profile, producing
FT mannotriose and mannose from mannotetraose, compared to
FT predominantly mannobiose in the wild type."
FT /evidence="ECO:0000269|Ref.7"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1QNR"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 205..221
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:1QNR"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:1QNR"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:1QNR"
SQ SEQUENCE 437 AA; 47053 MW; 17513DADE12654A7 CRC64;
MMMLSKSLLS AATAASALAA VLQPVPRASS FVTISGTQFN IDGKVGYFAG TNCYWCSFLT
NHADVDSTFS HISSSGLKVV RVWGFNDVNT QPSPGQIWFQ KLSATGSTIN TGADGLQTLD
YVVQSAEQHN LKLIIPFVNN WSDYGGINAY VNAFGGNATT WYTNTAAQTQ YRKYVQAVVS
RYANSTAIFA WELGNEPRCN GCSTDVIVQW ATSVSQYVKS LDSNHLVTLG DEGLGLSTGD
GAYPYTYGEG TDFAKNVQIK SLDFGTFHLY PDSWGTNYTW GNGWIQTHAA ACLAAGKPCV
FEEYGAQQNP CTNEAPWQTT SLTTRGMGGD MFWQWGDTFA NGAQSNSDPY TVWYNSSNWQ
CLVKNHVDAI NGGTTTPPPV SSTTTTSSRT SSTPPPPGGS CSPLYGQCGG SGYTGPTCCA
QGTCIYSNYW YSQCLNT
