MANA_PODAN
ID MANA_PODAN Reviewed; 373 AA.
AC B2B3C0; E2GHW1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase A;
DE EC=3.2.1.78 {ECO:0000269|PubMed:21037302};
DE AltName: Full=Endo-beta-1,4-mannanase A;
DE AltName: Full=Man5A;
DE Flags: Precursor;
GN OrderedLocusNames=Pa_6_490; ORFNames=PODANS_6_490;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-373, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=21037302; DOI=10.1128/aem.01761-10;
RA Couturier M., Haon M., Coutinho P.M., Henrissat B., Lesage-Meessen L.,
RA Berrin J.G.;
RT "Podospora anserina hemicellulases potentiate the Trichoderma reesei
RT secretome for saccharification of lignocellulosic biomass.";
RL Appl. Environ. Microbiol. 77:237-246(2011).
RN [4] {ECO:0007744|PDB:3ZIZ}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS), FUNCTION, DISULFIDE BONDS, SUBUNIT,
RP ACTIVE SITE, AND MUTAGENESIS OF GLU-194 AND GLU-300.
RX PubMed=23558681; DOI=10.1074/jbc.m113.459438;
RA Couturier M., Roussel A., Rosengren A., Leone P., Stalbrand H.,
RA Berrin J.G.;
RT "Structural and biochemical analyses of glycoside hydrolase families 5 and
RT 26 beta-(1,4)-mannanases from Podospora anserina reveal differences upon
RT manno-oligosaccharide catalysis.";
RL J. Biol. Chem. 288:14624-14635(2013).
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. Hydrolyzes structurally different mannan
CC polysaccharides, such as galactomannans, glucomannans, and beta-1,4-
CC mannans from different sources, yielding principally mannobiose
CC (PubMed:21037302). Also has transglycosylation activity
CC (PubMed:23558681). {ECO:0000269|PubMed:21037302,
CC ECO:0000269|PubMed:23558681}.
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:21037302};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mg/ml for konjac glucomannan {ECO:0000269|PubMed:21037302};
CC KM=1.7 mg/ml for carob galactomannan {ECO:0000269|PubMed:21037302};
CC KM=4.7 mg/ml for locust bean gum galactomannan
CC {ECO:0000269|PubMed:21037302};
CC KM=1.6 mg/ml for ivory nut mannan {ECO:0000269|PubMed:21037302};
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:21037302};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:21037302};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23558681}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99036}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:23558681}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; CU638744; CAP71606.1; -; Genomic_DNA.
DR EMBL; FO904941; CDP31001.1; -; Genomic_DNA.
DR EMBL; HM357135; ADO14134.1; -; mRNA.
DR RefSeq; XP_001910471.1; XM_001910436.1.
DR PDB; 3ZIZ; X-ray; 1.40 A; A=18-373.
DR PDBsum; 3ZIZ; -.
DR AlphaFoldDB; B2B3C0; -.
DR SMR; B2B3C0; -.
DR STRING; 5145.XP_001910471.1; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; MAN5A_PODAN; -.
DR EnsemblFungi; CAP71606; CAP71606; PODANS_6_490.
DR GeneID; 6194921; -.
DR KEGG; pan:PODANSg7509; -.
DR VEuPathDB; FungiDB:PODANS_6_490; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_4_1_1; -.
DR OrthoDB; 1003648at2759; -.
DR BRENDA; 3.2.1.78; 4930.
DR Proteomes; UP000001197; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; PTHR31451; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..373
FT /note="Mannan endo-1,4-beta-mannosidase A"
FT /id="PRO_5007639352"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:23558681"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:23558681"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT DISULFID 197..200
FT /evidence="ECO:0000269|PubMed:23558681,
FT ECO:0007744|PDB:3ZIZ"
FT DISULFID 289..296
FT /evidence="ECO:0000269|PubMed:23558681,
FT ECO:0007744|PDB:3ZIZ"
FT DISULFID 308..359
FT /evidence="ECO:0000269|PubMed:23558681,
FT ECO:0007744|PDB:3ZIZ"
FT MUTAGEN 194
FT /note="E->A: Reduces catalytic activity 100-fold."
FT /evidence="ECO:0000269|PubMed:23558681"
FT MUTAGEN 300
FT /note="E->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:23558681"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 203..219
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 278..292
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 307..320
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT TURN 321..325
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:3ZIZ"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:3ZIZ"
SQ SEQUENCE 373 AA; 41183 MW; 6902ACE6C55FCACA CRC64;
MKGLFAFGLG LLSLVNALPQ AQGGGAAASA KVSGTRFVID GKTGYFAGTN SYWIGFLTNN
RDVDTTLDHI ASSGLKILRV WGFNDVNNQP SGNTVWFQRL ASSGSQINTG PNGLQRLDYL
VRSAETRGIK LIIALVNYWD DFGGMKAYVN AFGGTKESWY TNARAQEQYK RYIQAVVSRY
VNSPAIFAWE LANEPRCKGC NTNVIFNWAT QISDYIRSLD KDHLITLGDE GFGLPGQTTY
PYQYGEGTDF VKNLQIKNLD FGTFHMYPGH WGVPTSFGPG WIKDHAAACR AAGKPCLLEE
YGYESDRCNV QKGWQQASRE LSRDGMSGDL FWQWGDQLST GQTHNDGFTI YYGSSLATCL
VTDHVRAINA LPA
