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D4GYH1 (AGLF_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UTP--glucose-1-phosphate uridylyltransferase AglF

EC=2.7.7.9
Alternative name(s):
Archaeal glycosylation protein F
Gene names
Name:aglF
Ordered Locus Names:HVO_1527
OrganismHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Reference proteome] [HAMAP]
Taxonomic identifier309800 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acid found at position 3 of the pentasaccharide. Ref.1 Ref.3 Ref.4

Catalytic activity

UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose. Ref.3

Pathway

Cell surface structure biogenesis; S-layer biogenesis. Ref.3

Disruption phenotype

Mutants exhibit defective or limited motility. Ref.4

Sequence similarities

Belongs to the UDPGP type 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243UTP--glucose-1-phosphate uridylyltransferase AglF
PRO_0000415423

Sequences

Sequence LengthMass (Da)Tools
D4GYH1 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 6AA3AC63E053AA35

FASTA24327,535
        10         20         30         40         50         60 
MQAVVLAAGK GTRLRPLTED KPKGMVEVDG KPILTHCFDQ LVDLGAEKLV VVVGYKKEII 

        70         80         90        100        110        120 
IQHYDDEYRG VPITYAHQRE QKGLAHALLT VEDHIDEDFM LMLGDNIFNA NLGDVVKRQR 

       130        140        150        160        170        180 
EDRADAAFLV EEVDWDEASR YGVCVTNDYG EITEVIEKPE EPPSNLVMTG FYTFTPAIFH 

       190        200        210        220        230        240 
ACHLVQPSNR GEYEISEAID LLIRSGRTID AIRIDGWRLD IGYPEDRDEA EQRLQEETTQ 


ATE 

« Hide

References

« Hide 'large scale' references
[1]"AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein."
Yurist-Doutsch S., Abu-Qarn M., Battaglia F., Morris H.R., Hitchen P.G., Dell A., Eichler J.
Mol. Microbiol. 69:1234-1245(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN GLYCOSYLATION, GENE NAME.
Strain: DS2 / DS70.
[2]"The complete genome sequence of Haloferax volcanii DS2, a model archaeon."
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.
PLoS ONE 5:E9605-E9605(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[3]"N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM."
Yurist-Doutsch S., Magidovich H., Ventura V.V., Hitchen P.G., Dell A., Eichler J.
Mol. Microbiol. 75:1047-1058(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
Strain: DS2 / DS70.
[4]"N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella."
Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.
J. Bacteriol. 194:4876-4887(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN GLYCOSYLATION OF FLAGELLINS, DISRUPTION PHENOTYPE.
Strain: H53.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM991128 Genomic DNA. Translation: CAQ51229.1.
CP001956 Genomic DNA. Translation: ADE04323.1.
RefSeqYP_003535574.1. NC_013967.1.

3D structure databases

ProteinModelPortalD4GYH1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE04323; ADE04323; HVO_1527.
GeneID8924609.
KEGGhvo:HVO_1527.

Phylogenomic databases

HOGENOMHOG000283477.
KOK00973.
OMAILTHCFD.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-1530-MONOMER.
UniPathwayUPA00977.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGLF_HALVD
AccessionPrimary (citable) accession number: D4GYH1
Secondary accession number(s): B2G4W5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 18, 2010
Last modified: June 11, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways