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Protein

Mannan endo-1,4-beta-mannosidase C

Gene

manC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.1 Publication

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei196 – 1961Proton donorBy similarity
Active sitei313 – 3131NucleophileBy similarity

GO - Molecular functioni

  1. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB

GO - Biological processi

  1. mannan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi3.2.1.78. 517.

Protein family/group databases

mycoCLAPiMAN5C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase C (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase C
Gene namesi
Name:manC
ORF Names:AN6427
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome I

Subcellular locationi

  1. Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 399381Mannan endo-1,4-beta-mannosidase CPRO_0000393710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5AZ53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
InParanoidiQ5AZ53.
OMAiVEWSNQW.
OrthoDBiEOG7C2R9T.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5AZ53-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIFSTLLSLA LLATTATARK GFVTTKGDKF QLDGKDFYFA GSNAYYFPFN
60 70 80 90 100
NNQTDVELGL SAAKKAGLLV FRTWGFNDKN VTYIEDGLPQ YGGEGAGTTE
110 120 130 140 150
VVFQWWQNGT STIDLEPFDK VVNAAAKTGI KLIVTLVNNW ADYGGMDVYT
160 170 180 190 200
VNLGGQYHDD FYRLPQIKKA YKRYVKEMVT RYRNSPAIMA WELANEPRCG
210 220 230 240 250
ADGVRNLPAS DECTPELLTS WIDEMSTYVK RLDPHHLVTW GGEGGFNYDS
260 270 280 290 300
DDWAYNGSDG GDFEAELKLK NIDFGVFHSY PDWWSKTVEW TNKWIVDHAR
310 320 330 340 350
AARRVGKPVV HEEYGWLTPQ GRLDNLGTVS NITRLEAVGG WQSISLREKM
360 370 380 390
SDMFWQFGYS GYSYGRNHDD GFTIYLDDAE AQELVYKHAK EVNKLNRRR
Length:399
Mass (Da):45,338
Last modified:April 26, 2005 - v1
Checksum:i9898F0BF644934CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490502 mRNA. Translation: ABF50878.1.
AACD01000108 Genomic DNA. Translation: EAA58449.1.
BN001301 Genomic DNA. Translation: CBF69494.1.
RefSeqiXP_664031.1. XM_658939.1.

Genome annotation databases

EnsemblFungiiCADANIAT00006551; CADANIAP00006551; CADANIAG00006551.
GeneIDi2871320.
KEGGiani:AN6427.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490502 mRNA. Translation: ABF50878.1.
AACD01000108 Genomic DNA. Translation: EAA58449.1.
BN001301 Genomic DNA. Translation: CBF69494.1.
RefSeqiXP_664031.1. XM_658939.1.

3D structure databases

ProteinModelPortaliQ5AZ53.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiMAN5C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00006551; CADANIAP00006551; CADANIAG00006551.
GeneIDi2871320.
KEGGiani:AN6427.2.

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
InParanoidiQ5AZ53.
OMAiVEWSNQW.
OrthoDBiEOG7C2R9T.

Enzyme and pathway databases

BRENDAi3.2.1.78. 517.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiMANC_EMENI
AccessioniPrimary (citable) accession number: Q5AZ53
Secondary accession number(s): C8V0G0, Q1HFS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: April 1, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.