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Q5NPH0 (GLND_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:ZMO0766
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length926 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 – 926926Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231700

Regions

Domain523 – 61795HD
Domain737 – 81478ACT 1
Domain849 – 92678ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 736357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q5NPH0 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: A854FC1B043AD4BE

FASTA926104,393
        10         20         30         40         50         60 
MPVSFLSLAS QPQIIDYPAI KEEIDSIKKV AAGDPVSEYR AVSLVLKQTV LKGREVIAEA 

        70         80         90        100        110        120 
LTRRPHQGRI AALSYAYLTD QIIQLALYAM VGDDEKATDN LVILAVGGYG RGEMALHSDV 

       130        140        150        160        170        180 
DIAFLSRRSP RKAQKKLIES LISLLWDVGL RVSQSHRSLS DMVKMAKKDI TIRTALLESR 

       190        200        210        220        230        240 
YLVGDKALFE EASTRFIQKV VAGSGRDFVA AKLLEWDERH LARGDSRYLV EPHLKEGKGG 

       250        260        270        280        290        300 
LRDLQSLFWI AKYLYLEKEA RHTVLTSPIL TDYALVKADL IAGHEAKRFR RCENFLWAVR 

       310        320        330        340        350        360 
CHLHILVKRP EERLNFDVQR SLAEKMGYRS KSGKSAVERF MHHYFLVTKM VGNLAALFID 

       370        380        390        400        410        420 
ALKVNHYLKP KSRRSGASKQ IDGFPVIQGE IVLDDDFFFR HNPAALITLF AVAYRHRLDI 

       430        440        450        460        470        480 
HPLTLRQAGR DARLIDEALQ NNPVCNAAFL TLFTLPYNPA PILKIMNNTG VLGRFIPDFG 

       490        500        510        520        530        540 
RIVAQMQFDM YHHYTVDEHA IRALDILWQI ENNKLEDLYP LGSRLFKQLN ARLVLYMALF 

       550        560        570        580        590        600 
LHDIAKGREG SHSALGAEIA LRLCPRFGLT AAETKLVAWL VKNHLLMSHT AFQRDLADAK 

       610        620        630        640        650        660 
TITDFANAVK SPERLRLLYL LTVADISAVG PHIWNSWKNQ LLTSLYEACS QCLLEGPTGH 

       670        680        690        700        710        720 
GAGRQQRIEN RQNDVSEKLD WDNDLFHALV KRLPDDYWFS ERTDVIAANM QQIIDTDSKG 

       730        740        750        760        770        780 
QSISVRGHEM PAYDATMISL YAIDHPGFFY RISGAIHATG GNILDARIHT TRDGMAMDNL 

       790        800        810        820        830        840 
LVQNSQGGMI KSGEHLNRMM QAIEDAATSH IRSSNKLAAL RPPLFWRGKA FHVEPLVFID 

       850        860        870        880        890        900 
NQASDRFTVI EVNAQDRPAL LHDLGCALFN ARLTISSAHI ATYGERAVDV FYVSDLFSHK 

       910        920 
ITNQNRLKAI EKRLLAAADA ARISEK 

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References

[1]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008692 Genomic DNA. Translation: AAV89390.1.
RefSeqYP_162501.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ5NPH0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO0766.

Proteomic databases

PRIDEQ5NPH0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89390; AAV89390; ZMO0766.
GeneID3188782.
KEGGzmo:ZMO0766.
PATRIC32566842. VBIZymMob102260_0725.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05092.

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]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF08335. 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_ZYMMO
AccessionPrimary (citable) accession number: Q5NPH0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 62 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