MANB_EMENI
ID MANB_EMENI Reviewed; 387 AA.
AC Q5B833; C8VI04; Q1HFT9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase B;
DE EC=3.2.1.78 {ECO:0000269|PubMed:16844780};
DE AltName: Full=Beta-mannanase 5B;
DE Short=Man5B {ECO:0000303|PubMed:24950755};
DE AltName: Full=Endo-beta-1,4-mannanase B;
DE Flags: Precursor;
GN Name=manB; ORFNames=AN3297;
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], AND FUNCTION.
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 PROTEIN SEQUENCE OF 25-29, 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 efficient transglycosylation activity.
CC Produces mainly mannopentaose and mannoheptaose out of mannotetraose.
CC May even prefer sugars as acceptors instead of water (PubMed:24950755).
CC {ECO:0000269|PubMed:16844780, 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=0.6 mg/ml for locust bean gum mannan
CC {ECO:0000269|PubMed:24950755};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:24950755};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:24950755};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF83007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA63265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490485; ABF50861.1; -; mRNA.
DR EMBL; AACD01000055; EAA63265.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF83007.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_660901.1; XM_655809.1.
DR AlphaFoldDB; Q5B833; -.
DR SMR; Q5B833; -.
DR STRING; 162425.CADANIAP00009761; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; MAN5A_EMENI; -.
DR PRIDE; Q5B833; -.
DR EnsemblFungi; EAA63265; EAA63265; AN3297.2.
DR GeneID; 2873762; -.
DR KEGG; ani:AN3297.2; -.
DR VEuPathDB; FungiDB:AN3297; -.
DR eggNOG; ENOG502QQFD; Eukaryota.
DR HOGENOM; CLU_031603_4_1_1; -.
DR InParanoid; Q5B833; -.
DR OrthoDB; 1003648at2759; -.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:24950755"
FT CHAIN 25..387
FT /note="Mannan endo-1,4-beta-mannosidase B"
FT /id="PRO_0000393708"
FT ACT_SITE 204
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 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 240
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 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 207..210
FT /evidence="ECO:0000250|UniProtKB:Q99036"
SQ SEQUENCE 387 AA; 43725 MW; 8CC8A4C1253E7823 CRC64;
MRLIHAVLGL LAGAAPALVA ASPAAPIGNG RDQVSKAVGR HFEIDGKVQY FAGTNCWWLG
NLLNDFEVEL AVSQIAETGY KVVRTWGFFG VNDPSNPGQP VYYQVLNESL YEGGLGINYG
SNGIRRLDTV VSLAERYDIQ LVLTFMNNWN DFGGINIYSN AFGSNATTWY TDKKSQRAYR
EYIKFIVNRY KGSSAIFAWE LGNEPRCKGC DPSVIYNWAK SVSAYIKKLD KKHMVALGDE
GWLCPPEGDG TYAYDCSEGV DFVKNLEIET LDYGTFHLYP ESWGYNYSWG SEWVLQHDAI
GKRFNKPVVF EEYGTPLNHT QLERPWQLTT VKETQVAADF IWQFGTVLPV EGTEWGDVNS
IYYGTEEYEV LAVQHAWEMA RKKVPRH
