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Mannan endo-1,4-beta-mannosidase A (EC 3.2.1.78) (Beta-mannanase 5A) (Man5A) (Beta-mannanase I/II) (BMANI) (BMANII) (Endo-beta-1,4-mannanase A)

 MANA_HYPJR              Reviewed;         437 AA.
Q99036; A0A024SIJ3;
30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 97.
RecName: Full=Mannan endo-1,4-beta-mannosidase A;
EC=3.2.1.78 {ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3, ECO:0000269|Ref.4};
AltName: Full=Beta-mannanase 5A;
Short=Man5A {ECO:0000303|PubMed:12523968};
AltName: Full=Beta-mannanase I/II {ECO:0000303|PubMed:8529653};
Short=BMANI;
Short=BMANII;
AltName: Full=Endo-beta-1,4-mannanase A;
Flags: Precursor;
Name=man1 {ECO:0000303|PubMed:7793911};
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut
C-30) (Trichoderma reesei).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
Trichoderma.
NCBI_TaxID=1344414;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE OF 28-42.
STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
PubMed=7793911;
Staalbrand H., Saloheimo A., Vehmaanperae J., Henrissat B.,
Penttilae M.;
"Cloning and expression in Saccharomyces cerevisiae of a Trichoderma
reesei beta-mannanase gene containing a cellulose binding domain.";
Appl. Environ. Microbiol. 61:1090-1097(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
DOI=10.1089/ind.2013.0015;
Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
"Comparative genomics analysis of Trichoderma reesei strains.";
Ind. Biotechnol. 9:352-367(2013).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
DOI=10.1007/BF00166849;
Arisan-Atac I., Hodits R., Kristufek D., Kubicek C.P.;
"Purification, and characterization of a beta-mannanase of Trichoderma
reesei C-30.";
Appl. Microbiol. Biotechnol. 39:58-62(1993).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
DOI=10.1016/0168-1656(93)90055-R;
Staalbrand H.;
"Purification and characterization of two beta-mannanases from
Trichoderma reesei.";
J. Biotechnol. 29:229-242(1993).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=8529653; DOI=10.1111/j.1432-1033.1995.278_c.x;
Harjunpaeae V., Teleman A., Siika-Aho M., Drakenberg T.;
"Kinetic and stereochemical studies of manno-oligosaccharide
hydrolysis catalysed by beta-mannanases from Trichoderma reesei.";
Eur. J. Biochem. 234:278-283(1995).
[6]
DOMAIN.
STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
PubMed=12523968; DOI=10.1016/S0168-1656(02)00290-0;
Haegglund P., Eriksson T., Collen A., Nerinckx W., Claeyssens M.,
Staalbrand H.;
"A cellulose-binding module of the Trichoderma reesei beta-mannanase
Man5A increases the mannan-hydrolysis of complex substrates.";
J. Biotechnol. 101:37-48(2003).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-198.
DOI=10.3109/10242422.2012.674726;
Rosengren A., Haegglund P., Anderson L., Pavon-Orozco P.,
Peterson-Wulff R., Nerinckx W., Staalbrand H.;
"The role of subsite +2 of the Trichoderma reesei beta-mannanase
TrMan5A in hydrolysis and transglycosylation.";
Biocatal. Biotransformation 30:338-352(2012).
[8]
FUNCTION.
PubMed=24950755; DOI=10.1007/s00253-014-5871-8;
Rosengren A., Reddy S.K., Sjoeberg J.S., Aurelius O., Logan D.T.,
Kolenova K., Staalbrand H.;
"An Aspergillus nidulans beta-mannanase with high transglycosylation
capacity revealed through comparative studies within glycosidase
family 5.";
Appl. Microbiol. Biotechnol. 98:10091-10104(2014).
[9] {ECO:0000244|PDB:1QNO, ECO:0000244|PDB:1QNP, ECO:0000244|PDB:1QNQ}
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 28-371 IN COMPLEX WITH
MANNOBIOSE, GLYCOSYLATION AT ASN-157; ASN-184; ASN-277 AND ASN-355,
DISULFIDE BONDS, AND ACTIVE SITE.
PubMed=10666621; DOI=10.1107/S0907444999013943;
Sabini E., Schubert H., Murshudov G., Wilson K.S., Siika-Aho M.,
Penttila M.;
"The three-dimensional structure of a Trichoderma reesei beta-
mannanase from glycoside hydrolase family 5.";
Acta Crystallogr. D 56:3-13(2000).
-!- FUNCTION: Endo-1,4-mannanase that catalyzes the random hydrolysis
of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans.
It is a crucial enzyme for depolymerization of seed galactomannans
and wood galactoglucomannans. Active against locust bean gum and
ivory nut mannan, releasing mainly tri- and disaccharides
(PubMed:7793911, Ref.3, Ref.4, PubMed:8529653). Also has
transglycosylation activity. Transglycosylation of two
mannotrioses into a mannohexaose is the major transglycosylation
route (PubMed:8529653, Ref.7, PubMed:24950755).
{ECO:0000269|PubMed:24950755, ECO:0000269|PubMed:7793911,
ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3, ECO:0000269|Ref.4,
ECO:0000269|Ref.7}.
-!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-beta-D-mannosidic
linkages in mannans, galactomannans and glucomannans.
{ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3,
ECO:0000269|Ref.4}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.0015 mg/ml for locust bean gum mannan {ECO:0000269|Ref.3};
KM=0.6 mg/ml for locust bean gum mannan {ECO:0000269|Ref.7};
KM=0.25 mM for 4-methylumbelliferyl-mannotrioside
{ECO:0000269|Ref.7};
KM=0.31 mM for mannotetraose {ECO:0000269|Ref.7};
KM=0.08 mM for mannopentaose {ECO:0000269|Ref.7};
KM=0.05 mM for mannohexaose {ECO:0000269|Ref.7};
pH dependence:
Optimum pH is 5.0. Stable from pH 2.5 to 7.0.
{ECO:0000269|Ref.3};
Temperature dependence:
Optimum temperature is 75 degrees Celsius. {ECO:0000269|Ref.3};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:B2B3C0}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3,
ECO:0000269|Ref.4}.
-!- DOMAIN: The enzyme consists of two functional domains, a catalytic
core joined to a carbohydrate-binding domain (CBM) by a serine-,
threonine-, and proline-rich, highly glycosylated linker sequence
(Probable). The CBM binds to cellulose but not to mannan, and
increases the mannan-hydrolysis of complex substrates
(PubMed:12523968). {ECO:0000269|PubMed:12523968,
ECO:0000305|PubMed:7793911}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L25310; AAA34208.1; -; mRNA.
EMBL; KI911141; ETS04541.1; -; Genomic_DNA.
PDB; 1QNO; X-ray; 2.00 A; A=28-371.
PDB; 1QNP; X-ray; 1.50 A; A=28-371.
PDB; 1QNQ; X-ray; 1.65 A; A=28-371.
PDB; 1QNR; X-ray; 1.40 A; A=28-371.
PDB; 1QNS; X-ray; 1.50 A; A=28-371.
PDBsum; 1QNO; -.
PDBsum; 1QNP; -.
PDBsum; 1QNQ; -.
PDBsum; 1QNR; -.
PDBsum; 1QNS; -.
ProteinModelPortal; Q99036; -.
SMR; Q99036; -.
STRING; 51453.JGI56996; -.
CAZy; CBM1; Carbohydrate-Binding Module Family 1.
CAZy; GH5; Glycoside Hydrolase Family 5.
EnsemblFungi; ETS04541; ETS04541; M419DRAFT_122377.
eggNOG; ENOG410IIG3; Eukaryota.
eggNOG; COG3934; LUCA.
EvolutionaryTrace; Q99036; -.
Proteomes; UP000024376; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030248; F:cellulose binding; IEA:InterPro.
GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
InterPro; IPR035971; CBD_sf.
InterPro; IPR000254; Cellulose-bd_dom_fun.
InterPro; IPR001547; Glyco_hydro_5.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00734; CBM_1; 1.
Pfam; PF00150; Cellulase; 1.
ProDom; PD001821; CBD_fun; 1.
SMART; SM00236; fCBD; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF57180; SSF57180; 1.
PROSITE; PS00562; CBM1_1; 1.
PROSITE; PS51164; CBM1_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Secreted;
Signal.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 27 {ECO:0000269|PubMed:7793911}.
/FTId=PRO_0000441278.
CHAIN 28 437 Mannan endo-1,4-beta-mannosidase A.
/FTId=PRO_5004322683.
DOMAIN 400 435 CBM1. {ECO:0000255|PROSITE-
ProRule:PRU00597}.
REGION 28 376 Catalytic. {ECO:0000305|PubMed:7793911}.
REGION 196 198 Substrate binding. {ECO:0000244|PDB:1QNR,
ECO:0000269|PubMed:10666621}.
REGION 377 399 Linker. {ECO:0000305|PubMed:7793911}.
ACT_SITE 196 196 Proton donor/acceptor.
{ECO:0000305|PubMed:10666621}.
ACT_SITE 303 303 Nucleophile.
{ECO:0000305|PubMed:10666621}.
BINDING 232 232 Substrate. {ECO:0000244|PDB:1QNR,
ECO:0000269|PubMed:10666621}.
BINDING 274 274 Substrate. {ECO:0000244|PDB:1QNR,
ECO:0000269|PubMed:10666621}.
SITE 198 198 Important for transglycosylation
activity. {ECO:0000269|Ref.7}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
/FTId=CAR_5009973567.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
/FTId=CAR_5009973566.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
/FTId=CAR_5009973568.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
/FTId=CAR_5009973565.
DISULFID 53 56 {ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
DISULFID 199 202 {ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
DISULFID 292 299 {ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
DISULFID 311 361 {ECO:0000244|PDB:1QNO,
ECO:0000244|PDB:1QNP,
ECO:0000244|PDB:1QNQ,
ECO:0000269|PubMed:10666621}.
MUTAGEN 198 198 R->K: Shows an altered product profile,
producing mannotriose and mannose from
mannotetraose, compared to predominantly
mannobiose in the wild type.
{ECO:0000269|Ref.7}.
STRAND 33 35 {ECO:0000244|PDB:1QNR}.
STRAND 38 41 {ECO:0000244|PDB:1QNR}.
STRAND 44 46 {ECO:0000244|PDB:1QNR}.
STRAND 48 52 {ECO:0000244|PDB:1QNR}.
HELIX 54 58 {ECO:0000244|PDB:1QNR}.
HELIX 62 74 {ECO:0000244|PDB:1QNR}.
STRAND 79 81 {ECO:0000244|PDB:1QNR}.
STRAND 87 90 {ECO:0000244|PDB:1QNR}.
STRAND 99 101 {ECO:0000244|PDB:1QNR}.
TURN 113 116 {ECO:0000244|PDB:1QNR}.
HELIX 117 129 {ECO:0000244|PDB:1QNR}.
STRAND 132 137 {ECO:0000244|PDB:1QNR}.
STRAND 139 142 {ECO:0000244|PDB:1QNR}.
HELIX 146 154 {ECO:0000244|PDB:1QNR}.
HELIX 160 163 {ECO:0000244|PDB:1QNR}.
HELIX 165 182 {ECO:0000244|PDB:1QNR}.
STRAND 188 193 {ECO:0000244|PDB:1QNR}.
HELIX 205 221 {ECO:0000244|PDB:1QNR}.
STRAND 223 228 {ECO:0000244|PDB:1QNR}.
HELIX 243 245 {ECO:0000244|PDB:1QNR}.
STRAND 246 250 {ECO:0000244|PDB:1QNR}.
HELIX 253 257 {ECO:0000244|PDB:1QNR}.
STRAND 264 269 {ECO:0000244|PDB:1QNR}.
HELIX 271 274 {ECO:0000244|PDB:1QNR}.
HELIX 281 294 {ECO:0000244|PDB:1QNR}.
STRAND 299 304 {ECO:0000244|PDB:1QNR}.
HELIX 310 322 {ECO:0000244|PDB:1QNR}.
STRAND 327 333 {ECO:0000244|PDB:1QNR}.
HELIX 357 362 {ECO:0000244|PDB:1QNR}.
HELIX 364 370 {ECO:0000244|PDB:1QNR}.
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


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