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Protein

Mannan endo-1,4-beta-mannosidase 5

Gene

MAN5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei214 – 2141Proton donorBy similarity
Active sitei334 – 3341NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. seed germination Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciARA:AT4G28320-MONOMER.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MAN5
Ordered Locus Names:At4g28320
ORF Names:F26K10.200
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G28320.

Subcellular locationi

Secreted Curated

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 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 431407Mannan endo-1,4-beta-mannosidase 5PRO_0000277478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9M0H6.
PRIDEiQ9M0H6.

Expressioni

Tissue specificityi

Expressed in stems.1 Publication

Gene expression databases

GenevestigatoriQ9M0H6.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G28320.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9M0H6.
SMRiQ9M0H6. Positions 41-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169952.
InParanoidiQ9M0H6.
OMAiDMEEFHD.
PhylomeDBiQ9M0H6.

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.

Q9M0H6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPTRNRPML RILGFFICAA FIYLSFRDLW LNHKGKAKLG FVKRNGTQFV
60 70 80 90 100
VDDKPLYVNG WNSYWFMDHA VDEHSRNLVG EMLEAGAKMG LTVCRTWAFN
110 120 130 140 150
DGGYNALQIS PGRFDERVFQ ALDHVIAEAR KHDVRLLLSL VNNLQAYGGK
160 170 180 190 200
TQYVKWAWQE GVGLSSSNDS FFFDPSIRNY FKNYLKVLLT RKNSVTGIEY
210 220 230 240 250
RNDPTIFAWE LINEPRCTTD VSGKTLQDWI DEMTGFIKSI DDKHLLTVGL
260 270 280 290 300
EGFYGPNSPK GLTVNPEQWA SQLGTDFVQN SNSSNIDFAS VHIYPDHWFH
310 320 330 340 350
NQTFEEKLKF VVKWMQSHIE DGLKELKKPV LFTEFGLSNQ NKDYEPSQRD
360 370 380 390 400
KFYRIIFDVV YKSAKRKKSG AGTLVWQLFM EGMETFNDDF GIVPHEQDSI
410 420 430
YKLMIEQSCR LGKVTGRLKE QKLKELCSHR H
Length:431
Mass (Da):49,899
Last modified:October 1, 2000 - v1
Checksum:i3EEDCC0BE61EC90A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161572 Genomic DNA. Translation: CAB79634.1.
CP002687 Genomic DNA. Translation: AEE85469.1.
AK228732 mRNA. Translation: BAF00634.1.
BT026124 mRNA. Translation: ABG48480.1.
PIRiT09048.
RefSeqiNP_194561.1. NM_118972.4.
UniGeneiAt.48910.
At.71248.

Genome annotation databases

EnsemblPlantsiAT4G28320.1; AT4G28320.1; AT4G28320.
GeneIDi828947.
KEGGiath:AT4G28320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161572 Genomic DNA. Translation: CAB79634.1.
CP002687 Genomic DNA. Translation: AEE85469.1.
AK228732 mRNA. Translation: BAF00634.1.
BT026124 mRNA. Translation: ABG48480.1.
PIRiT09048.
RefSeqiNP_194561.1. NM_118972.4.
UniGeneiAt.48910.
At.71248.

3D structure databases

ProteinModelPortaliQ9M0H6.
SMRiQ9M0H6. Positions 41-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G28320.1-P.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Proteomic databases

PaxDbiQ9M0H6.
PRIDEiQ9M0H6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G28320.1; AT4G28320.1; AT4G28320.
GeneIDi828947.
KEGGiath:AT4G28320.

Organism-specific databases

TAIRiAT4G28320.

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169952.
InParanoidiQ9M0H6.
OMAiDMEEFHD.
PhylomeDBiQ9M0H6.

Enzyme and pathway databases

BioCyciARA:AT4G28320-MONOMER.

Gene expression databases

GenevestigatoriQ9M0H6.

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. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
    , 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.
  4. "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.
  5. "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] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMAN5_ARATH
AccessioniPrimary (citable) accession number: Q9M0H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. 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.