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Protein

Mannan endo-1,4-beta-mannosidase 4

Gene

MAN4

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.2 Publications

Catalytic activityi

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

pH dependencei

Optimum pH is 5.0 for both endo-beta-mannanase and mannan transglycosylase activities.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei204Proton donorBy similarity1
Active sitei318NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.78. 3101.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase 4 (EC:3.2.1.78)
Alternative name(s):
Beta-mannanase 4
Endo-beta-1,4-mannanase 4
LeMAN4a
LeMAN4i
Gene namesi
Name:MAN4
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
Proteomesi
  • UP000004994 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi394 – 399RLSKLS → ALS: Activity reduced by 5-fold. 1 Publication6
Mutagenesisi394R → A: Activity slightly reduced. 1
Mutagenesisi396 – 399Missing : Activity reduced by 8-fold. 4
Mutagenesisi397 – 399Missing : Activity reduced by 3-fold. 3
Mutagenesisi398 – 399Missing : Activity reduced by 5-fold. 2
Mutagenesisi399Missing : No effect on activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000027749227 – 399Mannan endo-1,4-beta-mannosidase 4Add BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi347 ↔ 3541 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ8L5J1.

Expressioni

Tissue specificityi

Expressed in flowers and fruit pericarp.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc01g008710.2.1.

Structurei

Secondary structure

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 36Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi45 – 47Combined sources3
Beta strandi49 – 53Combined sources5
Helixi57 – 62Combined sources6
Turni64 – 67Combined sources4
Helixi68 – 79Combined sources12
Beta strandi84 – 90Combined sources7
Beta strandi92 – 96Combined sources5
Beta strandi98 – 101Combined sources4
Helixi107 – 122Combined sources16
Beta strandi126 – 130Combined sources5
Beta strandi133 – 140Combined sources8
Helixi141 – 150Combined sources10
Helixi158 – 162Combined sources5
Helixi165 – 180Combined sources16
Turni184 – 186Combined sources3
Helixi190 – 192Combined sources3
Beta strandi196 – 201Combined sources6
Helixi214 – 230Combined sources17
Beta strandi233 – 237Combined sources5
Helixi246 – 251Combined sources6
Helixi253 – 255Combined sources3
Helixi262 – 266Combined sources5
Beta strandi274 – 277Combined sources4
Helixi280 – 283Combined sources4
Helixi289 – 310Combined sources22
Beta strandi314 – 318Combined sources5
Helixi330 – 349Combined sources20
Beta strandi353 – 360Combined sources8
Helixi368 – 370Combined sources3
Helixi378 – 380Combined sources3
Helixi382 – 395Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RH9X-ray1.50A27-399[»]
ProteinModelPortaliQ8L5J1.
SMRiQ8L5J1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8L5J1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIVS. Eukaryota.
COG3934. LUCA.
InParanoidiQ8L5J1.
KOiK19355.
OMAiWATETSA.
OrthoDBiEOG09360BHK.

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.

Q8L5J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNSIILIFV AILIIFPNEF SKPTRAFSNN NFVYTDGTHF ALNGKSLYIN
60 70 80 90 100
GFNAYWLMYI AYDPSTRIKV TNTFQQASKY KMNVARTWAF SHGGSRPLQS
110 120 130 140 150
APGVYNEQMF QGLDFVISEA KKYGIHLIMS LVNNWDAFGG KKQYVEWAVQ
160 170 180 190 200
RGQKLTSDDD FFTNPMVKGF YKNNVKVVLT RVNTITKVAY KDDPTILSWE
210 220 230 240 250
LINEPRCPSD LSGKTFQNWV LEMAGYLKSI DSNHLLEIGL EGFYGNDMRQ
260 270 280 290 300
YNPNSYIFGT NFISNNQVQG IDFTTIHMYP NQWLPGLTQE AQDKWASQWI
310 320 330 340 350
QVHIDDSKML KKPLLIAEFG KSTKTPGYTV AKRDNYFEKI YGTIFNCAKS
360 370 380 390
GGPCGGGLFW QVLGQGMSSF DDGYQVVLQE SPSTSRVILL QSLRLSKLS
Length:399
Mass (Da):45,339
Last modified:February 6, 2007 - v2
Checksum:i805A7D7866E5FF6B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti274T → A in AAK56557 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti394 – 399RLSKLS → AL in strain: cv. Castalia and cv. Walter; in allele LeMAN4i; inactive enzyme. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046588 mRNA. Translation: AAK97760.1.
AY046589 mRNA. Translation: AAK97759.2.
AY034075 mRNA. Translation: AAK56557.1.
RefSeqiNP_001234131.1. NM_001247202.2.
UniGeneiLes.22467.
Les.25883.
Les.25913.

Genome annotation databases

EnsemblPlantsiSolyc01g008710.2.1; Solyc01g008710.2.1; Solyc01g008710.2.
GeneIDi543823.
GrameneiSolyc01g008710.2.1; Solyc01g008710.2.1; Solyc01g008710.2.
KEGGisly:543823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046588 mRNA. Translation: AAK97760.1.
AY046589 mRNA. Translation: AAK97759.2.
AY034075 mRNA. Translation: AAK56557.1.
RefSeqiNP_001234131.1. NM_001247202.2.
UniGeneiLes.22467.
Les.25883.
Les.25913.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RH9X-ray1.50A27-399[»]
ProteinModelPortaliQ8L5J1.
SMRiQ8L5J1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc01g008710.2.1.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Proteomic databases

PaxDbiQ8L5J1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiSolyc01g008710.2.1; Solyc01g008710.2.1; Solyc01g008710.2.
GeneIDi543823.
GrameneiSolyc01g008710.2.1; Solyc01g008710.2.1; Solyc01g008710.2.
KEGGisly:543823.

Phylogenomic databases

eggNOGiENOG410IIVS. Eukaryota.
COG3934. LUCA.
InParanoidiQ8L5J1.
KOiK19355.
OMAiWATETSA.
OrthoDBiEOG09360BHK.

Enzyme and pathway databases

BRENDAi3.2.1.78. 3101.

Miscellaneous databases

EvolutionaryTraceiQ8L5J1.

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 nameiMAN4_SOLLC
AccessioniPrimary (citable) accession number: Q8L5J1
Secondary accession number(s): Q8RVL3, Q93WT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: November 2, 2016
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.