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A5WCX0 (GLND_PSYWF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. 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:PsycPRwf_0556
OrganismPsychrobacter sp. (strain PRwf-1) [Complete proteome] [HAMAP]
Taxonomic identifier349106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length899 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 899899Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000071929

Regions

Domain494 – 57784HD
Domain719 – 80486ACT 1
Domain827 – 89973ACT 2
Region1 – 347347Uridylyltransferase HAMAP-Rule MF_00277
Region348 – 718371Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A5WCX0 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 52396B5DE7317311

FASTA899103,339
        10         20         30         40         50         60 
MFISDPTDSL ITPLPDLTAH SEAQSRNLGI PDWLKQIEAD IATALEKGVD IRHLVEARAA 

        70         80         90        100        110        120 
SIDSLLIELF KLHELTQTDL ALFAVGGYGR GELSPYSDVD ILILSPDTLS AEISQKVDGF 

       130        140        150        160        170        180 
VARLWDVGIE PGIAVRTIED CLQVATDITV ATNLLEARLL IGNDSLSAIP NNVVQQTWSQ 

       190        200        210        220        230        240 
KEFYDAKMAE ARARHLLHNG TEYNLEPDIK KSPGGLRDIH TIGWITKRYF RITKLYDLVP 

       250        260        270        280        290        300 
QDFLTEKEFD ELMFAEGFLW RIRHHLHHLT GRNENKLLFD YQRDIAERMG YEQSEEDEPN 

       310        320        330        340        350        360 
AAVENFMRDY YRCAMQISTL SEMLTSHYYE TLIEARLPES ERPEKSVLNA RFNRVGDHIA 

       370        380        390        400        410        420 
IAHHHVFAQH PEAILEMFLL MGQHGIKHIR TRTLRALKIA ARGIDQHYRD NPLHKKLFLD 

       430        440        450        460        470        480 
NLKEQNYLFH RLRIMKRYGV LANYMPQFVN LIGLMQYDLF HRYTVDAHIL LLIRMLHRFT 

       490        500        510        520        530        540 
SPKYQDDFAL VGSIYKRIER KEIIVLAAIF HDIAKGRGGD HSELGERDAI EFCLSHGMSE 

       550        560        570        580        590        600 
ADAKLIGWLT RYHLLMSMTA QKQDISDPEV VTKFANLVGN VTHLNHLYVL TVADMNATNP 

       610        620        630        640        650        660 
QLWNSWRASL MKQLYTQTRR ILRADLDAPT NRQEMIATTR QQALTMLDKV DNQHMNREEV 

       670        680        690        700        710        720 
LALWDELGDE YFLREIPEAI MWHTEAILNH PPIGRASDAN SEPLIVLREH RELALDAVQI 

       730        740        750        760        770        780 
FIYTQDQANL FAVTMAVFDQ MNLDVLDARI ITATRDFALD SYVLLDRHGT LLTDPESREE 

       790        800        810        820        830        840 
LTRRLIDAFK NPETPKLVQK RLPRRLKNFQ VPTTIDFNYN EASRQHVMSL TTLDQPGLLA 

       850        860        870        880        890 
RIGQVFLNEG IEVHAARITT LGERAEDMFY ISDIGDNMLS DAKLERLRTT LIDVLTPSC 

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References

[1]"Complete sequence of chromosome of Psychrobacter sp. PRwf-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PRwf-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000713 Genomic DNA. Translation: ABQ93511.1.
RefSeqYP_001279461.1. NC_009524.1.

3D structure databases

ProteinModelPortalA5WCX0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349106.PsycPRwf_0556.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ93511; ABQ93511; PsycPRwf_0556.
GeneID5204669.
KEGGprw:PsycPRwf_0556.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPPRW349106:GHZF-566-MONOMER.

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_PSYWF
AccessionPrimary (citable) accession number: A5WCX0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 53 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