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Q9KPV0 (GLND_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzyme

Short name=UTase/UR
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein

Including the following 2 domains:

  1. [Protein-PII] uridylyltransferase
    Short name=PII uridylyltransferase
    Short name=UTase
    EC=2.7.7.59
  2. [Protein-PII]-UMP uridylyl-removing enzyme
    Short name=UR
    EC=3.1.4.-
Gene names
Name:glnD
Ordered Locus Names:VC_2262
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length876 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism By similarity. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

Domain

Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing By similarity. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence caution

The sequence AAF95406.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 876876Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192771

Regions

Domain451 – 584134HD
Domain693 – 77785ACT 1
Domain800 – 87677ACT 2
Region1 – 332332Uridylyltransferase HAMAP-Rule MF_00277
Region333 – 692360Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q9KPV0 [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: D7A48AB39C755C32

FASTA876101,542
        10         20         30         40         50         60 
MPYQSPITFQ EPQLTVESLK QQLESFTEYQ KQEFFDHHPV TDLVLGRSEY MDLLLHRLWQ 

        70         80         90        100        110        120 
FFGFDELVEV SLVAVGGYGR GELHPLSDID LLVLSQQPLS EQVANKISQF LTLLWDLKLE 

       130        140        150        160        170        180 
IGHAVRTVEQ CAEIGKADLT VATNLQEARL LCGCEETFHR LKMVIHSESF WPSEIFYQAK 

       190        200        210        220        230        240 
VREQKERHAR YHDTTYNLEP DIKSTPGGLR DIHTLSWVAR RHFGATSLYE MSRFGFLTDA 

       250        260        270        280        290        300 
EYRELVECQD FLWRVRFALH IELKRYDNRL TFAHQVQVAR HLGYFGEGNR GIEMMMKEFF 

       310        320        330        340        350        360 
RTLRRVAELN KMLLKIFDKA ILNNGEEAEA VIIDDDFQRR GNMIEARKPA LFQARPETIL 

       370        380        390        400        410        420 
DMFLHMASDS TIESVAPATM RQLRTARRRL NKFLHTLPAA REKFIELVRH PNALHKAFSQ 

       430        440        450        460        470        480 
MHKLGVLAAY LPQWNQIVGQ MQFDLFHVYT VDEHSIRLLK HIHLFSDANN HDRHPICCEI 

       490        500        510        520        530        540 
YPKIQKKELL ILAAIFHDIG KGRGGDHSEI GADEAFDFCI EHGLSKPEAK LVAWLVKNHL 

       550        560        570        580        590        600 
LMSVTAQRRD IYDPDVIIEF AKKVRDEERL EYLVCLTVAD ICATNPELWN SWKRTLLAEL 

       610        620        630        640        650        660 
FYSTQRALRR GLENPVDVRE RIRHNQQMAS ALLRKEGFSS REIEVLWQRF KADYFLRHTH 

       670        680        690        700        710        720 
KQIAWHCTHL LRHEDSSKPL VLLSKKATRG GTEVFIYTKD QAALFATVVA ELDRRNLNVH 

       730        740        750        760        770        780 
DAQIMASKDG YVLDTFMVLD QNGQAIEEDR HQALIRHLVH VLEDGRPTTQ KARRIPRNLQ 

       790        800        810        820        830        840 
HFKVKTQVDF LPTKSKKRTL MEFVALDTPG LLATVGATFA ELNLDLHAAK ITTIGERAED 

       850        860        870 
LFILTNAQGT RLNEEEEQHL REKLIEHVAE LAPSAQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF95406.1. Different initiation.
PIRE82097.
RefSeqNP_231893.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KPV0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC2262.

Protocols and materials databases

DNASU2613184.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF95406; AAF95406; VC_2262.
GeneID2613184.
KEGGvch:VC2262.
PATRIC20083567. VBIVibCho83274_2158.

Phylogenomic databases

eggNOGCOG2844.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_VIBCH
AccessionPrimary (citable) accession number: Q9KPV0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 85 of the entry and version 2 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