MANC_EMENI
ID MANC_EMENI Reviewed; 399 AA.
AC Q5AZ53; C8V0G0; Q1HFS2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase C;
DE EC=3.2.1.78 {ECO:0000269|PubMed:16844780};
DE AltName: Full=Endo-beta-1,4-mannanase C;
DE Flags: Precursor;
GN Name=manC; ORFNames=AN6427;
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 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. Produces
CC mainly mannopentaose and mannohexaose out of mannotetraose
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=3.1 mg/ml for locust bean gum mannan
CC {ECO:0000269|PubMed:24950755};
CC KM=1.8 mM for mannopentaose {ECO:0000269|PubMed:21867780};
CC KM=0.6 mM for mannohexaose {ECO:0000269|PubMed:21867780};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:21867780};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:21867780};
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; DQ490502; ABF50878.1; -; mRNA.
DR EMBL; AACD01000108; EAA58449.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF69494.1; -; Genomic_DNA.
DR RefSeq; XP_664031.1; XM_658939.1.
DR AlphaFoldDB; Q5AZ53; -.
DR SMR; Q5AZ53; -.
DR STRING; 162425.CADANIAP00006551; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; MAN5C_EMENI; -.
DR PRIDE; Q5AZ53; -.
DR EnsemblFungi; CBF69494; CBF69494; ANIA_06427.
DR EnsemblFungi; EAA58449; EAA58449; AN6427.2.
DR GeneID; 2871320; -.
DR KEGG; ani:AN6427.2; -.
DR VEuPathDB; FungiDB:AN6427; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_4_0_1; -.
DR InParanoid; Q5AZ53; -.
DR OMA; QRWMEEM; -.
DR OrthoDB; 1003648at2759; -.
DR BRENDA; 3.2.1.78; 517.
DR Proteomes; UP000000560; Chromosome I.
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..399
FT /note="Mannan endo-1,4-beta-mannosidase C"
FT /id="PRO_0000393710"
FT ACT_SITE 196
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 196..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 199..213
FT /evidence="ECO:0000250|UniProtKB:Q99036"
SQ SEQUENCE 399 AA; 45338 MW; 9898F0BF644934CE CRC64;
MIFSTLLSLA LLATTATARK GFVTTKGDKF QLDGKDFYFA GSNAYYFPFN NNQTDVELGL
SAAKKAGLLV FRTWGFNDKN VTYIEDGLPQ YGGEGAGTTE VVFQWWQNGT STIDLEPFDK
VVNAAAKTGI KLIVTLVNNW ADYGGMDVYT VNLGGQYHDD FYRLPQIKKA YKRYVKEMVT
RYRNSPAIMA WELANEPRCG ADGVRNLPAS DECTPELLTS WIDEMSTYVK RLDPHHLVTW
GGEGGFNYDS DDWAYNGSDG GDFEAELKLK NIDFGVFHSY PDWWSKTVEW TNKWIVDHAR
AARRVGKPVV HEEYGWLTPQ GRLDNLGTVS NITRLEAVGG WQSISLREKM SDMFWQFGYS
GYSYGRNHDD GFTIYLDDAE AQELVYKHAK EVNKLNRRR
