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Protein

Probable mannan endo-1,4-beta-mannosidase F

Gene

manF

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

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 sitei305 – 3051NucleophileBy similarity

GO - Molecular functioni

  1. cellulose binding Source: InterPro
  2. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Probable mannan endo-1,4-beta-mannosidase F (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase F
Gene namesi
Name:manF
ORF Names:AO090038000444
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 6

Subcellular locationi

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 – 463445Probable mannan endo-1,4-beta-mannosidase FPRO_0000393716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2U2I3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 11844Ser-rich linkerAdd
BLAST
Regioni119 – 463345CatalyticrAdd
BLAST

Domaini

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
OMAiKYFAGTN.
OrthoDBiEOG7M3J90.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q2U2I3-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MRSLSSIALL SVVGAASAQA GPWAQCGGKS FSGSSECASG WKCQELNEWF
60 70 80 90 100
SQCVPGAEST TPTVSSTPTP TDAPSVSITA SVTTGINKSI SVSSASKSTP
110 120 130 140 150
LPSSSSASPS PRPTGSGSFA KADGLQFSID GETKYFAGTN AYWLPFQMND
160 170 180 190 200
ADIDSVFDHL EQAGLKILRV WGFNDVNTAP SPGTVYFQLH DKEKGTSTIN
210 220 230 240 250
TGKDGLQRLD YVVAAAEKHG VKLIIPFVNS WDDYGGYNAY VKAYGGSKTE
260 270 280 290 300
WFTNEKIQSV YQAYIKAVVS RYRDSPAIFA WELGNEPRCS GCSTDVIHGW
310 320 330 340 350
ATKISAYIKS LDPNHMVALG DEGMGLTIGS DQSYPYGTSE GNDFEKNLAI
360 370 380 390 400
PDIDFGTLHL YTTDWGIKDN AWGNGWVENH AKACKAAGKP CLFEEYGMKG
410 420 430 440 450
NHCTDELKWQ KTSLSSGTAA DLIWQYGQQL STGESPKDAY SIFYGTDEWK
460
CAVMDHMENV NKN
Length:463
Mass (Da):49,992
Last modified:April 20, 2010 - v2
Checksum:i8926BA2E033A383B
GO

Sequence cautioni

The sequence BAE64232.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007169 Genomic DNA. Translation: BAE64232.1. Sequence problems.
RefSeqiXP_001825365.2. XM_001825313.2.

Genome annotation databases

GeneIDi5997460.
KEGGiaor:AOR_1_742074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007169 Genomic DNA. Translation: BAE64232.1. Sequence problems.
RefSeqiXP_001825365.2. XM_001825313.2.

3D structure databases

ProteinModelPortaliQ2U2I3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5997460.
KEGGiaor:AOR_1_742074.

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
OMAiKYFAGTN.
OrthoDBiEOG7M3J90.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiMANF_ASPOR
AccessioniPrimary (citable) accession number: Q2U2I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: January 7, 2015
This is version 55 of the entry and version 2 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.