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Protein

Mannosyl-oligosaccharide alpha-1,2-mannosidase

Gene

MSDC

Organism
Penicillium citrinum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.1 Publication

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.1 Publication

Cofactori

Ca2+By similarity

pH dependencei

Optimum pH is 5.0.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei375Proton donor1 Publication1
Metal bindingi501CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.113. 4608.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.
mycoCLAPiMSD47C1_PENCI.
MSD47C2_PENCI.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide alpha-1,2-mannosidase (EC:3.2.1.1131 Publication)
Alternative name(s):
Man(9)-alpha-mannosidase
Gene namesi
Name:MSDC
OrganismiPenicillium citrinum
Taxonomic identifieri5077 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 351 PublicationAdd BLAST35
ChainiPRO_000001208536 – 511Mannosyl-oligosaccharide alpha-1,2-mannosidaseAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi182N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi332 ↔ 361Combined sources1 Publication
Glycosylationi366N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi438N-linked (GlcNAc...)Combined sources1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 58Combined sources22
Turni59 – 61Combined sources3
Beta strandi62 – 66Combined sources5
Turni67 – 70Combined sources4
Beta strandi71 – 73Combined sources3
Turni75 – 78Combined sources4
Helixi81 – 93Combined sources13
Helixi96 – 108Combined sources13
Helixi120 – 139Combined sources20
Turni140 – 144Combined sources5
Helixi149 – 166Combined sources18
Helixi167 – 170Combined sources4
Beta strandi172 – 175Combined sources4
Beta strandi179 – 181Combined sources3
Turni183 – 185Combined sources3
Beta strandi192 – 195Combined sources4
Helixi196 – 200Combined sources5
Helixi203 – 213Combined sources11
Helixi217 – 230Combined sources14
Helixi235 – 237Combined sources3
Beta strandi246 – 249Combined sources4
Turni250 – 252Combined sources3
Turni264 – 266Combined sources3
Helixi267 – 279Combined sources13
Turni281 – 284Combined sources4
Helixi285 – 301Combined sources17
Beta strandi317 – 319Combined sources3
Beta strandi322 – 324Combined sources3
Beta strandi326 – 328Combined sources3
Helixi330 – 333Combined sources4
Helixi334 – 345Combined sources12
Helixi348 – 366Combined sources19
Beta strandi368 – 371Combined sources4
Beta strandi375 – 378Combined sources4
Turni381 – 383Combined sources3
Helixi386 – 388Combined sources3
Helixi389 – 395Combined sources7
Beta strandi398 – 401Combined sources4
Helixi409 – 421Combined sources13
Helixi424 – 440Combined sources17
Beta strandi444 – 447Combined sources4
Helixi456 – 458Combined sources3
Beta strandi459 – 463Combined sources5
Helixi468 – 471Combined sources4
Helixi473 – 479Combined sources7
Beta strandi496 – 499Combined sources4
Beta strandi505 – 507Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKTX-ray2.20A/B1-511[»]
1KREX-ray2.20A/B1-511[»]
1KRFX-ray2.20A/B1-511[»]
2RI8X-ray2.16A/B36-510[»]
2RI9X-ray1.95A/B36-510[»]
ProteinModelPortaliP31723.
SMRiP31723.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31723.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P31723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLPVSFPLT VLSLLGSTIA HPYGETEAVL RSEPKSNQAK ADAVKEAFQH
60 70 80 90 100
AWNGYMKYAF PHDELTPVSN GHADSRNGWG ASAVDALSTA VIMGKADVVN
110 120 130 140 150
AILEHVADID FSKTSDTVSL FETTIRYLAG MLSGYDLLQG PAKNLVDNQD
160 170 180 190 200
LIDGLLDQSR NLADVLKFAF DTPSGVPYNN INITSHGNDG ATTNGLAVTG
210 220 230 240 250
TLVLEWTRLS DLTGDEEYAK LSQKAESYLL KPQPSSSEPF PGLVGSSINI
260 270 280 290 300
NDGQFADSRV SWNGGDDSFY EYLIKMYVYD PKRFETYKDR WVLAAESTIK
310 320 330 340 350
HLKSHPKSRP DLTFLSSYSN RNYDLSSQHL TCFDGGSFLL GGTVLDRQDF
360 370 380 390 400
IDFGLELVDG CEATYNSTLT KIGPDSWGWD PKKVPSDQKE FYEKAGFYIS
410 420 430 440 450
SGSYVLRPEV IESFYYAHRV TGKEIYRDWV WNAFVAINST CRTDSGFAAV
460 470 480 490 500
SDVNKANGGS KYDNQESFLF AEVMKYSYLA HSEDAAWQVQ KGGKNTFVYN
510
TEAHPISVAR N
Length:511
Mass (Da):56,570
Last modified:October 1, 1996 - v2
Checksum:iDCBDEBA5768E7596
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti407R → H AA sequence (PubMed:8452520).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45839 Genomic DNA. Translation: BAA08275.1.
PIRiS30362.
S58766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45839 Genomic DNA. Translation: BAA08275.1.
PIRiS30362.
S58766.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKTX-ray2.20A/B1-511[»]
1KREX-ray2.20A/B1-511[»]
1KRFX-ray2.20A/B1-511[»]
2RI8X-ray2.16A/B36-510[»]
2RI9X-ray1.95A/B36-510[»]
ProteinModelPortaliP31723.
SMRiP31723.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.
mycoCLAPiMSD47C1_PENCI.
MSD47C2_PENCI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.113. 4608.

Miscellaneous databases

EvolutionaryTraceiP31723.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAN12_PENCI
AccessioniPrimary (citable) accession number: P31723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The enzyme is inactivated by reaction of carbodiimide reagents with Asp-375. Since the antibiotic 1-deoxymannojirimycin (DMM) acts as a competitive inhibitor, and it blocks the reaction with carbodiimides, Asp-375 is established as an active site. High activity in presence of EDTA.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.