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Q0BV39 (Q0BV39_GRABC) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 59. Feed History...

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

Protein namesRecommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277

Short name=UTase/UR HAMAP-Rule MF_00277
Alternative name(s):
Bifunctional [protein-PII] modification enzyme HAMAP-Rule MF_00277
Bifunctional nitrogen sensor protein HAMAP-Rule MF_00277
Gene names
Name:glnD HAMAP-Rule MF_00277
Ordered Locus Names:GbCGDNIH1_0415 EMBL ABI61313.1
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP] EMBL ABI61313.1
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter

Protein attributes

Sequence length963 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 SAAS SAAS013546

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277 SAAS SAAS013546

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. HAMAP-Rule MF_00277

Contains 1 HD domain. HAMAP-Rule MF_00277

Contains 2 ACT domains. HAMAP-Rule MF_00277

Contains ACT domains. SAAS SAAS013546

Contains HD domain. SAAS SAAS013546

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain520 – 631112HD By similarity HAMAP-Rule MF_00277
Domain756 – 83782ACT 1 By similarity HAMAP-Rule MF_00277
Domain869 – 95183ACT 2 By similarity HAMAP-Rule MF_00277
Region1 – 390390Uridylyltransferase By similarity HAMAP-Rule MF_00277
Region391 – 755365Uridylyl-removing By similarity HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q0BV39 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: FACD7A2CBB1E00F1

FASTA963106,130
        10         20         30         40         50         60 
MVTSSSPGLA QKAPRQTASE LAALELDRAL TALEEEFGPG PRKGPLSQLE RNAALGVFRR 

        70         80         90        100        110        120 
HLARIQGRVR DTFEQGRLAG LTAAHLLSDL TDGLVAALYQ YTDSIAIPAS ATQQTEPVTV 

       130        140        150        160        170        180 
AATGGYGRQE LAPFSDIDLL FITADTPSAR TLAVVEFMLY FLWDLGLKVG HATRSISQSL 

       190        200        210        220        230        240 
QAATEDTTVR TTLLDTRHLA GNQPLFDAFI TAFREACTEA GEHDFIAAKQ AERHARHLRY 

       250        260        270        280        290        300 
GESPFFVEPN IKEGRGGLRD LQTLYWLSRY VFGTRKLVDL VGTGAPGGGL ITENEARLAK 

       310        320        330        340        350        360 
RSWNFLWTLR FHLHYVAGRA EERLTFDVQP VIGARMGYTR HGRQNGVERF MRHYFLTARE 

       370        380        390        400        410        420 
VLRLTRVLEP ALIRAALGPP AIAAETDIAL INAGFVLAEG KLLPAPSHDF EREPIQMLRI 

       430        440        450        460        470        480 
MKLARDRDLQ IHPLGIRSLI RNERGAIALR DDQRAAALFL DLLCGNTVPD GVQRPTQRPS 

       490        500        510        520        530        540 
GARWMSILNE TGFLGRFIPE WARIVGQMQF DTYHVFTVDE HTIEAIRVLN QLEHGDLADI 

       550        560        570        580        590        600 
APVATGVVDH LQSRRALYVA MLTHDIAKGR GGDHSELGAE LALEIGPALG LDSEETEMVS 

       610        620        630        640        650        660 
WLVLHHLLLS QTAFRRDIDD PKTILDLADT IQSPERLKLL LVLTVADMRA VSSKVWNGWK 

       670        680        690        700        710        720 
ATLLRELYAR VAEVLAGGLA TTERDTRVAR AKEAAAELLY DWPEEQREAF LTLGYPGYWL 

       730        740        750        760        770        780 
SFDPETHARH ARMIRAAGTQ LLTVDTQPLP ARAVTEVTVY VADTPGLVGK IAGALAVAGA 

       790        800        810        820        830        840 
SIVDARIHTM TNGMAMDTFW VQDTSGEAFD QPNRLAKIAV LIEQALSGQL DIDEEIRKAS 

       850        860        870        880        890        900 
NPLLGTRMRA IHVPPRVVVD NHASHTHTVL EVNGRDRPGL MHDIAAAIAQ QGLQIASAHI 

       910        920        930        940        950        960 
TTYGVRAVDV FYVKDVFGLK VENERKLAKL RQALLGALTS PDDTGPMPLP PPMRRTHATG 


DDF 

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References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1260 / CGDNIH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000394 Genomic DNA. Translation: ABI61313.1.
RefSeqYP_744236.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BV39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391165.GbCGDNIH1_0415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI61313; ABI61313; GbCGDNIH1_0415.
GeneID4275199.
KEGGgbe:GbCGDNIH1_0415.
PATRIC22076889. VBIGraBet83793_0436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGBET391165:GHON-426-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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 nameQ0BV39_GRABC
AccessionPrimary (citable) accession number: Q0BV39
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)