MANA_EMENI
ID MANA_EMENI Reviewed; 383 AA.
AC Q5B7X2; C8VHS1; Q1HFT7;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase A;
DE EC=3.2.1.78 {ECO:0000269|PubMed:16844780};
DE AltName: Full=Endo-beta-1,4-mannanase A;
DE Flags: Precursor;
GN Name=manA; Synonyms=man1; ORFNames=AN3358;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21867780; DOI=10.1016/j.bbapap.2011.08.003;
RA Dilokpimol A., Nakai H., Gotfredsen C.H., Baumann M.J., Nakai N.,
RA Abou Hachem M., Svensson B.;
RT "Recombinant production and characterisation of two related GH5 endo-beta-
RT 1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly
RT different transglycosylation capacity.";
RL Biochim. Biophys. Acta 1814:1720-1729(2011).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24950755; DOI=10.1007/s00253-014-5871-8;
RA Rosengren A., Reddy S.K., Sjoeberg J.S., Aurelius O., Logan D.T.,
RA Kolenova K., Staalbrand H.;
RT "An Aspergillus nidulans beta-mannanase with high transglycosylation
RT capacity revealed through comparative studies within glycosidase family
RT 5.";
RL Appl. Microbiol. Biotechnol. 98:10091-10104(2014).
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. Active against locust bean gum and gum guar
CC (PubMed:16844780). Also has transglycosylation activity
CC (PubMed:21867780, PubMed:24950755). {ECO:0000269|PubMed:16844780,
CC ECO:0000269|PubMed:21867780, ECO:0000269|PubMed:24950755}.
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:16844780};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mg/ml for locust bean gum mannan
CC {ECO:0000269|PubMed:24950755};
CC KM=2.9 mM for mannopentaose {ECO:0000269|PubMed:21867780};
CC KM=1.8 mM for mannohexaose {ECO:0000269|PubMed:21867780};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:16844780,
CC ECO:0000269|PubMed:21867780};
CC Temperature dependence:
CC Optimum temperature is 52 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:B2B3C0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99036}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; DQ490487; ABF50863.1; -; mRNA.
DR EMBL; AACD01000055; EAA63326.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF82875.1; -; Genomic_DNA.
DR RefSeq; XP_660962.1; XM_655870.1.
DR AlphaFoldDB; Q5B7X2; -.
DR SMR; Q5B7X2; -.
DR STRING; 162425.CADANIAP00009689; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblFungi; CBF82875; CBF82875; ANIA_03358.
DR EnsemblFungi; EAA63326; EAA63326; AN3358.2.
DR GeneID; 2874351; -.
DR KEGG; ani:AN3358.2; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_4_1_1; -.
DR OMA; TMSKVTT; -.
DR OrthoDB; 1003648at2759; -.
DR BRENDA; 3.2.1.78; 517.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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 Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..383
FT /note="Mannan endo-1,4-beta-mannosidase A"
FT /id="PRO_0000393706"
FT ACT_SITE 211
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 214..217
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT DISULFID 301..308
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT DISULFID 320..369
FT /evidence="ECO:0000250|UniProtKB:Q99036"
SQ SEQUENCE 383 AA; 41789 MW; 686126F8B2CF12C1 CRC64;
MKFSQALLSL ASLALAAALP HASTPVYTPS TTPSPTPTPS ASGSFATTSG IQFVIDGEAG
YFPGSNAYWI GFLKNNSDVD LVFDHMASSG LRILRVWGFN DVNTAPTDGS VYFQLHQDGK
STINTGKDGL QRLDYVVHSA EKHGIKLIIN FVNYWDDYGG MNAYMRAYGG GDKADWFENE
GIQAAYQAYV EAVVKRYINS TAVFAWELAN EPRCTGCEPS VLHNWIEKTS AFIKGLDEKH
LVCIGDGSDG SYPFQYTEGS DFAAALTIDT IDFGTFHLYP DSWGTNNDWG KLWITSHAAA
CAAAGKPCLF EEYGVTSNHC AIEKQWQNAA LNATGIAADL YWQYGDTLSS GPSPDDGNTF
YYGSEEFECL VTNHVETIER SAK
