MANA_MYTED
ID MANA_MYTED Reviewed; 367 AA.
AC Q8WPJ2; P82544; P82801;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase;
DE EC=3.2.1.78;
DE AltName: Full=Beta-mannanase;
DE AltName: Full=Endo-beta-1,4-mannanase;
DE Short=Man5A;
DE Short=ManA;
DE Flags: Precursor;
OS Mytilus edulis (Blue mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6550 {ECO:0000312|EMBL:CAC81056.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Digestive gland {ECO:0000269|PubMed:11895446}, and
RC Gill {ECO:0000269|PubMed:11895446};
RX PubMed=11895446; DOI=10.1046/j.1432-1327.2002.02824.x;
RA Xu B., Sellos D., Janson J.-C.;
RT "Cloning and expression in Pichia pastoris of a blue mussel (Mytilus
RT edulis) beta-mannanase gene.";
RL Eur. J. Biochem. 269:1753-1760(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 18-53, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MASS SPECTROMETRY.
RC TISSUE=Digestive gland {ECO:0000269|PubMed:11689251};
RX PubMed=11689251; DOI=10.1016/s0168-1656(01)00367-4;
RA Xu B., Hagglund P., Stalbrand H., Janson J.-C.;
RT "endo-beta-1,4-mannanases from blue mussel, Mytilus edulis: purification,
RT characterization, and mode of action.";
RL J. Biotechnol. 92:267-277(2002).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=11856850; DOI=10.1107/s0907444902000355;
RA Xu B., Munoz I.G., Janson J.-C., Stahlberg J.;
RT "Crystallization and X-ray analysis of native and selenomethionyl beta-
RT mannanase Man5A from blue mussel, Mytilus edulis, expressed in Pichia
RT pastoris.";
RL Acta Crystallogr. D 58:542-545(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-367, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16487541; DOI=10.1016/j.jmb.2006.01.044;
RA Larsson A.M., Anderson L., Xu B., Munoz I.G., Uson I., Janson J.-C.,
RA Stalbrand H., Stahlberg J.;
RT "Three-dimensional crystal structure and enzymic characterization of beta-
RT mannanase Man5A from blue mussel Mytilus edulis.";
RL J. Mol. Biol. 357:1500-1510(2006).
CC -!- FUNCTION: Hydrolyzes 1,4-beta linked polysaccharide backbones of
CC mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose
CC (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5),
CC and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and
CC less preferentially to mannotetraose M4; hydrolyzes M4 preferentially
CC to M3, and less preferentially to mannose (M1), plus very little M2.
CC Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan,
CC starch, cellulose or galactose. {ECO:0000269|PubMed:11689251,
CC ECO:0000269|PubMed:11895446, ECO:0000269|PubMed:16487541}.
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=2.49 mM for mannotetraose {ECO:0000269|PubMed:11689251,
CC ECO:0000269|PubMed:16487541};
CC KM=1.61 mM for mannopentaose {ECO:0000269|PubMed:11689251,
CC ECO:0000269|PubMed:16487541};
CC KM=0.5 mM for mannohexaose {ECO:0000269|PubMed:11689251,
CC ECO:0000269|PubMed:16487541};
CC pH dependence:
CC Optimum pH is 5.2. {ECO:0000269|PubMed:11689251,
CC ECO:0000269|PubMed:16487541};
CC Temperature dependence:
CC Optimum temperature is about 50 degrees Celsius.
CC {ECO:0000269|PubMed:11689251, ECO:0000269|PubMed:16487541};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11689251}.
CC -!- PTM: The disulfide bond between Cys-192 and Cys-259 has not been
CC observed in x-ray crystallograghy (PubMed:16487541). This may be a
CC consequence of the X-ray radiation. {ECO:0000269|PubMed:16487541}.
CC -!- MASS SPECTROMETRY: Mass=39702; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11689251};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; AJ271365; CAC81056.1; -; Genomic_DNA.
DR PDB; 2C0H; X-ray; 1.60 A; A=15-367.
DR PDBsum; 2C0H; -.
DR AlphaFoldDB; Q8WPJ2; -.
DR SMR; Q8WPJ2; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PRIDE; Q8WPJ2; -.
DR BRENDA; 3.2.1.78; 3544.
DR EvolutionaryTrace; Q8WPJ2; -.
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; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:11689251"
FT CHAIN 18..367
FT /note="Mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000269|PubMed:11689251"
FT /id="PRO_0000007901"
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P07985"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07985"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT DISULFID 192..259
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="I -> M (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="I -> M (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2C0H"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 212..229
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2C0H"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:2C0H"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2C0H"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:2C0H"
SQ SEQUENCE 367 AA; 40957 MW; B364E03418D2EA86 CRC64;
MLLTALAVLF ASTGCQARLS VSGTNLNYNG HHIFLSGANQ AWVNYARDFG HNQYSKGKST
FESTLSDIQS HGGNSVRVWL HIEGESTPEF DNNGYVTGID NTLISDMRAY LHAAQRHNIL
IFFTLWNGAV KQSTHYRLNG LMVDTRKLQS YIDHALKPMA NALKNEKALG GWDIMNEPEG
EIKPGESSSE PCFDTRHLSG SGAGWAGHLY SAQEIGRFVN WQAAAIKEVD PGAMVTVGSW
NMKADTDAMG FHNLYSDHCL VKAGGKQSGT LSFYQVHTYD WQNHFGNESP FKHSFSNFRL
KKPMVIGEFN QEHGAGMSSE SMFEWAYTKG YSGAWTWSRT DVSWNNQLRG IQHLKSRTDH
GQVQFGL
