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Mannan endo-1,4-beta-mannosidase A (EC 3.2.1.78) (Endo-beta-1,4-mannanase A) (Man5A)

 MANA_PODAN              Reviewed;         373 AA.
B2B3C0; E2GHW1;
30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 1.
05-DEC-2018, entry version 61.
RecName: Full=Mannan endo-1,4-beta-mannosidase A;
EC=3.2.1.78 {ECO:0000269|PubMed:21037302};
AltName: Full=Endo-beta-1,4-mannanase A;
AltName: Full=Man5A;
Flags: Precursor;
OrderedLocusNames=Pa_6_490; ORFNames=PODANS_6_490;
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
(Pleurage anserina).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae;
Podospora.
NCBI_TaxID=515849;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O.,
Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J.,
Anthouard V., Grossetete S., Khalili H., Coppin E.,
Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A.,
Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E.,
Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R.,
Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
Debuchy R., Wincker P., Weissenbach J., Silar P.;
"The genome sequence of the model ascomycete fungus Podospora
anserina.";
Genome Biol. 9:R77.1-R77.22(2008).
[2]
GENOME REANNOTATION.
STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
PubMed=24558260; DOI=10.1534/genetics.113.159988;
Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E.,
Benkhali J.A., Couloux A., Wincker P., Debuchy R., Silar P.;
"Maintaining two mating types: Structure of the mating type locus and
its role in heterokaryosis in Podospora anserina.";
Genetics 197:421-432(2014).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-373, FUNCTION, CATALYTIC ACTIVITY,
AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
PubMed=21037302; DOI=10.1128/AEM.01761-10;
Couturier M., Haon M., Coutinho P.M., Henrissat B., Lesage-Meessen L.,
Berrin J.G.;
"Podospora anserina hemicellulases potentiate the Trichoderma reesei
secretome for saccharification of lignocellulosic biomass.";
Appl. Environ. Microbiol. 77:237-246(2011).
[4] {ECO:0000244|PDB:3ZIZ}
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS), FUNCTION, DISULFIDE BONDS,
SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF GLU-194 AND GLU-300.
PubMed=23558681; DOI=10.1074/JBC.M113.459438;
Couturier M., Roussel A., Rosengren A., Leone P., Stalbrand H.,
Berrin J.G.;
"Structural and biochemical analyses of glycoside hydrolase families 5
and 26 beta-(1,4)-mannanases from Podospora anserina reveal
differences upon manno-oligosaccharide catalysis.";
J. Biol. Chem. 288:14624-14635(2013).
-!- 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. Hydrolyzes structurally different
mannan polysaccharides, such as galactomannans, glucomannans, and
beta-1,4-mannans from different sources, yielding principally
mannobiose (PubMed:21037302). Also has transglycosylation activity
(PubMed:23558681). {ECO:0000269|PubMed:21037302,
ECO:0000269|PubMed:23558681}.
-!- CATALYTIC ACTIVITY:
Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
mannans, galactomannans and glucomannans.; EC=3.2.1.78;
Evidence={ECO:0000269|PubMed:21037302};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.7 mg/ml for konjac glucomannan
{ECO:0000269|PubMed:21037302};
KM=1.7 mg/ml for carob galactomannan
{ECO:0000269|PubMed:21037302};
KM=4.7 mg/ml for locust bean gum galactomannan
{ECO:0000269|PubMed:21037302};
KM=1.6 mg/ml for ivory nut mannan {ECO:0000269|PubMed:21037302};
pH dependence:
Optimum pH is 4.0. {ECO:0000269|PubMed:21037302};
Temperature dependence:
Optimum temperature is 60 degrees Celsius.
{ECO:0000269|PubMed:21037302};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23558681}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99036}.
-!- PTM: Not glycosylated. {ECO:0000269|PubMed:23558681}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; CU638744; CAP71606.1; -; Genomic_DNA.
EMBL; FO904941; CDP31001.1; -; Genomic_DNA.
EMBL; HM357135; ADO14134.1; -; mRNA.
RefSeq; XP_001910471.1; XM_001910436.1.
PDB; 3ZIZ; X-ray; 1.40 A; A=1-356.
PDBsum; 3ZIZ; -.
ProteinModelPortal; B2B3C0; -.
SMR; B2B3C0; -.
STRING; 515849.XP_001910471.1; -.
CAZy; GH5; Glycoside Hydrolase Family 5.
mycoCLAP; MAN5A_PODAN; -.
EnsemblFungi; CAP71606; CAP71606; PODANS_6_490.
GeneID; 6194921; -.
KEGG; pan:PODANSg7509; -.
eggNOG; ENOG410IIG3; Eukaryota.
eggNOG; COG3934; LUCA.
KO; K19355; -.
OrthoDB; EOG092C2KMO; -.
Proteomes; UP000001197; Chromosome 6.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
InterPro; IPR001547; Glyco_hydro_5.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00150; Cellulase; 1.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycosidase;
Hydrolase; Reference proteome; Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 373 Mannan endo-1,4-beta-mannosidase A.
/FTId=PRO_5007639352.
REGION 194 196 Substrate binding.
{ECO:0000250|UniProtKB:Q99036}.
ACT_SITE 194 194 Proton donor/acceptor.
{ECO:0000305|PubMed:23558681}.
ACT_SITE 300 300 Nucleophile.
{ECO:0000305|PubMed:23558681}.
BINDING 230 230 Substrate.
{ECO:0000250|UniProtKB:Q99036}.
BINDING 271 271 Substrate.
{ECO:0000250|UniProtKB:Q99036}.
DISULFID 197 200 {ECO:0000244|PDB:3ZIZ,
ECO:0000269|PubMed:23558681}.
DISULFID 289 296 {ECO:0000244|PDB:3ZIZ,
ECO:0000269|PubMed:23558681}.
DISULFID 308 359 {ECO:0000244|PDB:3ZIZ,
ECO:0000269|PubMed:23558681}.
MUTAGEN 194 194 E->A: Reduces catalytic activity 100-
fold. {ECO:0000269|PubMed:23558681}.
MUTAGEN 300 300 E->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:23558681}.
STRAND 30 33 {ECO:0000244|PDB:3ZIZ}.
STRAND 36 39 {ECO:0000244|PDB:3ZIZ}.
STRAND 42 44 {ECO:0000244|PDB:3ZIZ}.
STRAND 46 50 {ECO:0000244|PDB:3ZIZ}.
HELIX 54 56 {ECO:0000244|PDB:3ZIZ}.
HELIX 60 72 {ECO:0000244|PDB:3ZIZ}.
STRAND 77 81 {ECO:0000244|PDB:3ZIZ}.
STRAND 85 88 {ECO:0000244|PDB:3ZIZ}.
STRAND 97 99 {ECO:0000244|PDB:3ZIZ}.
TURN 102 104 {ECO:0000244|PDB:3ZIZ}.
TURN 111 113 {ECO:0000244|PDB:3ZIZ}.
HELIX 114 127 {ECO:0000244|PDB:3ZIZ}.
STRAND 130 134 {ECO:0000244|PDB:3ZIZ}.
STRAND 137 140 {ECO:0000244|PDB:3ZIZ}.
HELIX 144 152 {ECO:0000244|PDB:3ZIZ}.
HELIX 157 161 {ECO:0000244|PDB:3ZIZ}.
HELIX 163 180 {ECO:0000244|PDB:3ZIZ}.
STRAND 186 191 {ECO:0000244|PDB:3ZIZ}.
HELIX 203 219 {ECO:0000244|PDB:3ZIZ}.
STRAND 221 226 {ECO:0000244|PDB:3ZIZ}.
HELIX 240 242 {ECO:0000244|PDB:3ZIZ}.
HELIX 250 254 {ECO:0000244|PDB:3ZIZ}.
STRAND 261 266 {ECO:0000244|PDB:3ZIZ}.
HELIX 268 270 {ECO:0000244|PDB:3ZIZ}.
HELIX 275 277 {ECO:0000244|PDB:3ZIZ}.
HELIX 278 292 {ECO:0000244|PDB:3ZIZ}.
STRAND 296 301 {ECO:0000244|PDB:3ZIZ}.
STRAND 304 306 {ECO:0000244|PDB:3ZIZ}.
HELIX 307 320 {ECO:0000244|PDB:3ZIZ}.
TURN 321 325 {ECO:0000244|PDB:3ZIZ}.
STRAND 326 332 {ECO:0000244|PDB:3ZIZ}.
HELIX 355 360 {ECO:0000244|PDB:3ZIZ}.
HELIX 362 369 {ECO:0000244|PDB:3ZIZ}.
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


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