MAN5_SALAG
ID MAN5_SALAG Reviewed; 308 AA.
AC G1K3N4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000303|PubMed:19441796};
DE EC=3.2.1.78 {ECO:0000269|PubMed:19441796};
DE AltName: Full=Mannanase 5A {ECO:0000303|PubMed:19441796};
DE Short=Man5A {ECO:0000303|PubMed:19441796};
DE AltName: Full=Mannanase A {ECO:0000303|PubMed:19441796};
DE Short=ManA {ECO:0000303|PubMed:19441796};
OS Salipaludibacillus agaradhaerens (Bacillus agaradhaerens).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=76935;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=19441796; DOI=10.1021/bi900515d;
RA Tailford L.E., Ducros V.M., Flint J.E., Roberts S.M., Morland C.,
RA Zechel D.L., Smith N., Bjornvad M.E., Borchert T.V., Wilson K.S.,
RA Davies G.J., Gilbert H.J.;
RT "Understanding how diverse beta-mannanases recognize heterogeneous
RT substrates.";
RL Biochemistry 48:7009-7018(2009).
CC -!- FUNCTION: Catalyzes the endo hydrolysis of beta-1,4-linked mannan,
CC galactomannan and glucomannan. It is able to hydrolyze mannosidic
CC linkages that are flanked by mannose or glucose.
CC {ECO:0000269|PubMed:19441796}.
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:19441796};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mg/ml for galactomannan {ECO:0000269|PubMed:19441796};
CC KM=2.6 mg/ml for glucomannan {ECO:0000269|PubMed:19441796};
CC Note=kcat is 38000 min(-1) for mannanase activity with galactomannan
CC as substrate. kcat is 45000 min(-1) for mannanase activity with
CC glucomannan as substrate. {ECO:0000269|PubMed:19441796};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR PDB; 2WHJ; X-ray; 1.78 A; A=1-308.
DR PDBsum; 2WHJ; -.
DR AlphaFoldDB; G1K3N4; -.
DR SMR; G1K3N4; -.
DR EvolutionaryTrace; G1K3N4; -.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
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; Glycosidase; Hydrolase.
FT CHAIN 1..308
FT /note="Mannan endo-1,4-beta-mannosidase"
FT /id="PRO_0000433976"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P22533"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P22533"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:2WHJ"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2WHJ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2WHJ"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:2WHJ"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:2WHJ"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2WHJ"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2WHJ"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2WHJ"
SQ SEQUENCE 308 AA; 34211 MW; 2176B1022EF64742 CRC64;
AGFYVDGNTL YDANGQPFVM RGINHGHAWY KDTASTAIPA IAEQGANTIR IVLSDGGQWE
KDDIDTIREV IELAEQNKMV AVVEVHDATG RDSRSDLNRA VDYWIEMKDA LIGKEDTVII
NIANEWYGSW DGSAWADGYI DVIPKLRDAG LTHTLMVDAA GWGQYPQSIH DYGQDVFNAD
PLKNTMFSIH MYEYAGGDAN TVRSNIDRVI DQDLALVIGE FGHRHTDGDV DEDTILSYSE
ETGTGWLAWS WKGNSTEWDY LDLSEDWAGQ HLTDWGNRIV HGADGLQETS KPSTVFTDDN
GGHPEPPT
