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Protein

UDP-glucose 6-dehydrogenase AglM

Gene

aglM

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Activity improves as salinity decreases.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei269 – 2691By similarity

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. UDP-glucose 6-dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide biosynthetic process Source: InterPro
  2. S-layer organization Source: UniProtKB-UniPathway
  3. UDP-glucuronate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciHVOL309800:GCOK-1534-MONOMER.
BRENDAi1.1.1.22. 2561.
UniPathwayiUPA00038; UER00491.
UPA00977.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose 6-dehydrogenase AglM (EC:1.1.1.22)
Short name:
UDP-Glc dehydrogenase
Short name:
UDP-GlcDH
Short name:
UDPGDH
Alternative name(s):
Archaeal glycosylation protein M
Gene namesi
Name:aglM
Ordered Locus Names:HVO_1531
OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Taxonomic identifieri309800 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax
ProteomesiUP000008243 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Mutants exhibit defective or limited motility.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430UDP-glucose 6-dehydrogenase AglMPRO_0000415417Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliD4GYH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000153773.
KOiK00012.
OMAiAEEGVNH.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR008927. 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]
PANTHERiPTHR11374. PTHR11374. 1 hit.
PfamiPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.

Sequencei

Sequence statusi: Complete.

D4GYH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSIIGSGY VGTTIAACFA ELGHDVVNVD IDEDIVASLN DGQAPIHEPG
60 70 80 90 100
LAELVERYAG DRLRATTDYD EILDTDATFL ALPTPSTDDG SIDLGAMKTA
110 120 130 140 150
ATSLGETLAR KDDSHLVVTK STVVPRTTVD VIGPRIEEAS GKRVGDGLDI
160 170 180 190 200
AMNPEFLREG TAVDDFLSPD KIVLGAQTDR AYETLAEIFA PLVERAGNPP
210 220 230 240 250
VVKTGISEAE MIKYANNAFL ASKISLANDL ANICKVFGVD SAEVLESIGL
260 270 280 290 300
DSRIGSAFLG AGLGWGGSCF PKDTAAIIAA ARAQGYEPRL LQAAVDVNDG
310 320 330 340 350
QPERMLDLLR ERFDLDGKRV AVLGLAFKPG TDDIRKSRAI LLIQALLDAG
360 370 380 390 400
ADVVGYDPVA TENMRERFPD IDYADSAADA LANADAALVA TDWDEFAALD
410 420 430
DEFDAMRERI VIDGRRIVTR REGLDYESLV
Length:430
Mass (Da):45,967
Last modified:May 18, 2010 - v1
Checksum:iBC8ABB67E71DFF7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN386609 Genomic DNA. Translation: CAY46591.1.
CP001956 Genomic DNA. Translation: ADE05103.1.
RefSeqiWP_004041409.1. NZ_AOHU01000028.1.
YP_003535578.1. NC_013967.1.

Genome annotation databases

EnsemblBacteriaiADE05103; ADE05103; HVO_1531.
GeneIDi8924832.
KEGGihvo:HVO_1531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN386609 Genomic DNA. Translation: CAY46591.1.
CP001956 Genomic DNA. Translation: ADE05103.1.
RefSeqiWP_004041409.1. NZ_AOHU01000028.1.
YP_003535578.1. NC_013967.1.

3D structure databases

ProteinModelPortaliD4GYH5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE05103; ADE05103; HVO_1531.
GeneIDi8924832.
KEGGihvo:HVO_1531.

Phylogenomic databases

HOGENOMiHOG000153773.
KOiK00012.
OMAiAEEGVNH.

Enzyme and pathway databases

UniPathwayiUPA00038; UER00491.
UPA00977.
BioCyciHVOL309800:GCOK-1534-MONOMER.
BRENDAi1.1.1.22. 2561.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR008927. 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]
PANTHERiPTHR11374. PTHR11374. 1 hit.
PfamiPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, PATHWAY, GENE NAME.
    Strain: DS2 / DS70.
  2. 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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GLYCOSYLATION OF FLAGELLINS, DISRUPTION PHENOTYPE.
    Strain: H53.

Entry informationi

Entry nameiAGLM_HALVD
AccessioniPrimary (citable) accession number: D4GYH5
Secondary accession number(s): C3W971
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 18, 2010
Last modified: April 1, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.