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Reviewed, UniProtKB/Swiss-Prot Q9M0H6 (MAN5_ARATH)

Last modified October 13, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mannan endo-1,4-beta-mannosidase 5
    EC=3.2.1.78
Alternative name(s):
    Beta-mannanase 5
    Endo-beta-1,4-mannanase 5
      Short name=AtMAN5
Gene names
Name: MAN5
Ordered Locus Names: At4g28320
ORF Names: F26K10.200
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

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

Subcellular location

Secreted Potential.

Tissue specificity

Expressed in stems. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

mannan endo-1,4-beta-mannosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 431407Mannan endo-1,4-beta-mannosidase 5
PRO_0000277478

Sites

Active site2141Proton donor By similarity
Active site3341Nucleophile By similarity

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9M0H6-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3EEDCC0BE61EC90A

FASTA43149,899
        10         20         30         40         50         60 
MVPTRNRPML RILGFFICAA FIYLSFRDLW LNHKGKAKLG FVKRNGTQFV VDDKPLYVNG 

        70         80         90        100        110        120 
WNSYWFMDHA VDEHSRNLVG EMLEAGAKMG LTVCRTWAFN DGGYNALQIS PGRFDERVFQ 

       130        140        150        160        170        180 
ALDHVIAEAR KHDVRLLLSL VNNLQAYGGK TQYVKWAWQE GVGLSSSNDS FFFDPSIRNY 

       190        200        210        220        230        240 
FKNYLKVLLT RKNSVTGIEY RNDPTIFAWE LINEPRCTTD VSGKTLQDWI DEMTGFIKSI 

       250        260        270        280        290        300 
DDKHLLTVGL EGFYGPNSPK GLTVNPEQWA SQLGTDFVQN SNSSNIDFAS VHIYPDHWFH 

       310        320        330        340        350        360 
NQTFEEKLKF VVKWMQSHIE DGLKELKKPV LFTEFGLSNQ NKDYEPSQRD KFYRIIFDVV 

       370        380        390        400        410        420 
YKSAKRKKSG AGTLVWQLFM EGMETFNDDF GIVPHEQDSI YKLMIEQSCR LGKVTGRLKE 

       430 
QKLKELCSHR H

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Arabidopsis ORF clones."
Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"The endo-beta-mannanase gene families in Arabidopsis, rice, and poplar."
Yuan J.S., Yang X., Lai J., Lin H., Cheng Z.-M., Nonogaki H., Chen F.
Funct. Integr. Genomics 7:1-16(2007) [PubMed: 16897088] [Abstract]
Cited for: GENE FAMILY, TISSUE SPECIFICITY.

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Cross-references

Sequence databases

AL161572 Genomic DNA. Translation: CAB79634.1.
AK228732 mRNA. Translation: BAF00634.1.
BT026124 mRNA. Translation: ABG48480.1.
IPIIPI00535627.
PIRT09048.
RefSeqNP_194561.1.
UniGeneAt.48910

3D structure databases

HSSPHSSP built from PDB template 1QNR based on UniProtKB Q99036.
ModBaseSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Genome annotation databases

GeneID828947.
GenomeReviewsGene locus AT4G28320 in contig CT486007_GR.
KEGGath:AT4G28320.
NMPDRfig|3702.1.peg.20786.

Organism-specific databases

TAIRAt4g28320.

Enzyme and pathway databases

BRENDA3.2.1.78. 302.

Gene expression databases

ArrayExpressQ9M0H6.
GenevestigatorQ9M0H6.

Family and domain databases

InterProIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
PROSITEPS00659. GLYCOSYL_HYDROL_F5. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMAN5_ARATH
AccessionPrimary (citable) accession number: Q9M0H6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 1, 2000
Last modified: October 13, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents