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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)DescriptionActionsGraphical viewLength
Active sitei196Proton donorBy similarity1
Active sitei313NucleophileBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • 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

CAZyiGH5. Glycoside Hydrolase Family 5.
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
Proteomesi
  • UP000000560 Componenti: Chromosome I
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039371019 – 399Mannan endo-1,4-beta-mannosidase CAdd BLAST381

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi80N-linked (GlcNAc...)Sequence analysis1
Glycosylationi108N-linked (GlcNAc...)Sequence analysis1
Glycosylationi256N-linked (GlcNAc...)Sequence analysis1
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5AZ53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000169951.
InParanoidiQ5AZ53.
KOiK19355.
OMAiEVVFQRW.
OrthoDBiEOG092C2KMO.

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.
EAA58449; EAA58449; AN6427.2.
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

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiMAN5C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00006551; CADANIAP00006551; CADANIAG00006551.
EAA58449; EAA58449; AN6427.2.
GeneIDi2871320.
KEGGiani:AN6427.2.

Phylogenomic databases

HOGENOMiHOG000169951.
InParanoidiQ5AZ53.
KOiK19355.
OMAiEVVFQRW.
OrthoDBiEOG092C2KMO.

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...

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: November 30, 2016
This is version 71 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

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 one 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.