Mannosyl-oligosaccharide 1,2-alpha-mannosidase precursor - Caulobacter sp. (strain K31)

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B0SWV2 (B0SWV2_CAUSK) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 35. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase EMBL ABZ73160.1
EC=3.2.1.113 EMBL ABZ73160.1

Gene names

Ordered Locus Names:

Caul_4035 EMBL ABZ73160.1

Organism

Caulobacter sp. (strain K31) [Complete proteome] [HAMAP] EMBL ABZ73160.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Signal EMBL ABZ73160.1
Molecular function	Glycosidase EMBL ABZ73160.1 Hydrolase
Technical term	3D-structure PDB 4AYO PDB 4AYP PDB 4AYQ PDB 4AYR Complete proteome
Gene Ontology (GO)
Cellular_component	membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

26

Potential EMBL ABZ73160.1

Chain

436

Potential

PRO_5000307962

Sequences

Sequence

Length

Mass (Da)

Tools

B0SWV2 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: D20ECCB0C33D4ECC
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462

51,676

        10         20         30         40         50         60 
MTASHLSRRH ALALVASAAA APAFAAETTP EDWKALAADV RSEFQWAWQG YVAKAWGKDE 

        70         80         90        100        110        120 
INPVSGTSRS FFIEGHDLGL SLVEALDTLW IMGLDAEFQA GVDWVKANLS FDVDGNAQVF 

       130        140        150        160        170        180 
ETNIRLVGGL LSAHLASGDP VLLAKARDLA DRLAKAFEAS PHGLPWRYVN LRTGAVSDPE 

       190        200        210        220        230        240 
TNLAEIGTYL SEFGVLSQLT GERKYFDMAK RAMRHTLDRR SKIGLMAANI HAMTGAFTSR 

       250        260        270        280        290        300 
NASIDVYADS FYEYLWDAWA LFGDEDCKRW AVECVDAQLA HQAKRYDGRL WFPMVDFETG 

       310        320        330        340        350        360 
AVTGTAQSEL AAYYAGLLGQ VGRKAQGDDY LASFTYLQAT FGVIPESIDV TTGQPRRKHT 

       370        380        390        400        410        420 
GLRPEYPDAC LNLWLIDRDP RYRRLAAIHY REMKATSRAA FGYTALKDIT TRPMTQDDNC 

       430        440        450        460 
PGYWWSEQMK YYYLLFSDTP RIDYGQLQLS TEANVLRGFR KV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of chromosome of Caulobacter sp. K31." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Kim E., Stephens C., Richardson P. Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K31 EMBL ABZ73160.1.
[2]	"The reaction coordinate of a bacterial GH47 ?-mannosidase: a combined quantum mechanical and structural approach." Thompson A.J., Dabin J., Iglesias-Fernandez J., Ardevol A., Dinev Z., Williams S.J., Bande O., Siriwardena A., Moreland C., Hu T.C., Smith D.K., Gilbert H.J., Rovira C., Davies G.J. Angew. Chem. Int. Ed. 51:10997-11001(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 27-462.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000927 Genomic DNA. Translation: ABZ73160.1.

RefSeq

YP_001685658.1. NC_010338.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AYO	X-ray	0.85	A	27-462	[»]
4AYP	X-ray	0.85	A	27-462	[»]
4AYQ	X-ray	1.10	A	27-462	[»]
4AYR	X-ray	1.10	A	27-462	[»]

ProteinModelPortal

ModBase

Protein-protein interaction databases

STRING

366602.Caul_4035.

Protein family/group databases

CAZy

GH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

EnsemblBacteria

ABZ73160; ABZ73160; Caul_4035.

GeneID

KEGG

PATRIC

21321238. VBICauSp18104_4445.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

KO

OMA

ProtClustDB

Enzyme and pathway databases

BioCyc

CSP366602:GH0Y-4040-MONOMER.

Family and domain databases

Gene3D

1.50.10.50. 1 hit.

InterPro

IPR001382. Glyco_hydro_47.
IPR006311. TAT_signal.
[Graphical view]

PANTHER

PTHR11742. PTHR11742. 1 hit.

Pfam

PF01532. Glyco_hydro_47. 1 hit.
[Graphical view]

PRINTS

PR00747. GLYHDRLASE47.

SUPFAM

SSF48225. Glyco_hydro_47. 1 hit.

PROSITE

PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

B0SWV2_CAUSK

Accession

Primary (citable) accession number: B0SWV2

Entry history

Integrated into UniProtKB/TrEMBL:	April 8, 2008
Last sequence update:	April 8, 2008
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info