Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

D4GYH5 (AGLM_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 28. 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:
UDP-glucose 6-dehydrogenase AglM

Short name=UDP-Glc dehydrogenase
Short name=UDP-GlcDH
Short name=UDPGDH
EC=1.1.1.22
Alternative name(s):
Archaeal glycosylation protein M
Gene names
Name:aglM
Ordered Locus Names:HVO_1531
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 length430 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 acids found at both positions 2 and 3 of the pentasaccharide. Ref.1 Ref.3

Catalytic activity

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH. Ref.1

Enzyme regulation

Activity improves as salinity decreases. Ref.1

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. Ref.1

Cell surface structure biogenesis; S-layer biogenesis. Ref.1

Disruption phenotype

Mutants exhibit defective or limited motility. Ref.3

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430UDP-glucose 6-dehydrogenase AglM
PRO_0000415417

Sites

Active site2691 By similarity

Sequences

Sequence LengthMass (Da)Tools
D4GYH5 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: BC8ABB67E71DFF7F

FASTA43045,967
        10         20         30         40         50         60 
MELSIIGSGY VGTTIAACFA ELGHDVVNVD IDEDIVASLN DGQAPIHEPG LAELVERYAG 

        70         80         90        100        110        120 
DRLRATTDYD EILDTDATFL ALPTPSTDDG SIDLGAMKTA ATSLGETLAR KDDSHLVVTK 

       130        140        150        160        170        180 
STVVPRTTVD VIGPRIEEAS GKRVGDGLDI AMNPEFLREG TAVDDFLSPD KIVLGAQTDR 

       190        200        210        220        230        240 
AYETLAEIFA PLVERAGNPP VVKTGISEAE MIKYANNAFL ASKISLANDL ANICKVFGVD 

       250        260        270        280        290        300 
SAEVLESIGL DSRIGSAFLG AGLGWGGSCF PKDTAAIIAA ARAQGYEPRL LQAAVDVNDG 

       310        320        330        340        350        360 
QPERMLDLLR ERFDLDGKRV AVLGLAFKPG TDDIRKSRAI LLIQALLDAG ADVVGYDPVA 

       370        380        390        400        410        420 
TENMRERFPD IDYADSAADA LANADAALVA TDWDEFAALD DEFDAMRERI VIDGRRIVTR 

       430 
REGLDYESLV 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, PATHWAY, 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 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
FN386609 Genomic DNA. Translation: CAY46591.1.
CP001956 Genomic DNA. Translation: ADE05103.1.
RefSeqYP_003535578.1. NC_013967.1.

3D structure databases

ProteinModelPortalD4GYH5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE05103; ADE05103; HVO_1531.
GeneID8924832.
KEGGhvo:HVO_1531.

Phylogenomic databases

HOGENOMHOG000153773.
KOK00012.
OMANEVGNIC.
ProtClustDBCLSK510967.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-1534-MONOMER.
UniPathwayUPA00038; UER00491.
UPA00977.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR017476. UDP-Glc/GDP-Man.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
IPR028357. UDPglc_DH_bac.
[Graphical view]
PANTHERPTHR11374. PTHR11374. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGLM_HALVD
AccessionPrimary (citable) accession number: D4GYH5
Secondary accession number(s): C3W971
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 18, 2010
Last modified: December 11, 2013
This is version 28 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