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Q9XC07 (GLND_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. 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:VF_1964
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length873 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 – 873873Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192772

Regions

Domain451 – 584134HD
Domain693 – 77785ACT 1
Domain800 – 87374ACT 2
Region1 – 332332Uridylyltransferase HAMAP-Rule MF_00277
Region333 – 692360Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q9XC07 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 99CB3E00D0B5C568

FASTA873100,599
        10         20         30         40         50         60 
MKYLSPLSLS DTQLNITELK QQLTLFSQYQ INAFHQHKAV SDLVLERSHY FDQLLSRLWQ 

        70         80         90        100        110        120 
FFKFDDIANT SLIAVGGYGR SELHPLSDID ILILTENNTN DAFCQKVGEL VTLLWDLKLE 

       130        140        150        160        170        180 
VGHSVRSIAE CIEIGQNDLT VATNLQEARY ISGNKELSHQ LKLKIHSDSF WPSELFYQAK 

       190        200        210        220        230        240 
IDEQKKRHSR YHDTTYNLEP DIKSSPGGLR DIHTLSWIAR RHFGATSLLE MSQAGFLTDA 

       250        260        270        280        290        300 
EYRELLECQE FLWRVRFALH IELKRYDNRL TFGHQASVAE HLGFIGEGNR GVERMMKEFY 

       310        320        330        340        350        360 
RTLRRVAELN SMLLKIFDQA ILHQGEQDDA IIIDDDFQRR GRLIEARKPA LFQARPDTIL 

       370        380        390        400        410        420 
DMFLLMANDS TIDGVAPPTM RQLRTARRRL NRFLCEIPEA KEKFLQLTQH PNALNNAFSS 

       430        440        450        460        470        480 
MHKLGVLSAY LPQWSHIVGQ MQFDLFHAYT VDEHSIRLLK HINKFSDTTN RDKHPICCEI 

       490        500        510        520        530        540 
FPKIMKKELL IIAAIFHDIA KGRGGDHSEL GAVDAYDFCI SHGLSKPEAN LVSWLVKSHL 

       550        560        570        580        590        600 
LMSVTAQRRD IYDPDVITEF AKQVRDEERL DYLVCLTVAD ICATNPDLWN SWKRSLIADL 

       610        620        630        640        650        660 
YNATQRALRR GLENPPDLRD RIRHNQQMAS AQLRSEGFTQ WEVDALWRRF KADYFLRHTH 

       670        680        690        700        710        720 
KQIAWHASHL LRHQDKEKSL ILISKNASRG GTEIFVYSKD QPHLFATVAA ELDRRSITIY 

       730        740        750        760        770        780 
DAQVMSSKDG YALDTFMVLD QNDDPIDEER QQRLIDQLYD VKLNDQATHI KTRRPPRQLQ 

       790        800        810        820        830        840 
HFNVKTRMEF LPTKTGKRTL MEFVALDTPG LLATVGATFA QLGINLHAAK ITTIGERAED 

       850        860        870 
LFILTSDVGG RLDDEKQAEL ELALVKNVAR LSS 

« Hide

References

« Hide 'large scale' references
[1]"Unexpected effects of a transposon insertion in the Vibrio fischeri glnD gene: defects in iron uptake and symbiotic persistence in addition to nitrogen utilization."
Graf J., Ruby E.G.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152563 Genomic DNA. Translation: AAD38384.1.
CP000020 Genomic DNA. Translation: AAW86459.1.
RefSeqYP_205347.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ9XC07.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_1964.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW86459; AAW86459; VF_1964.
GeneID3279229.
KEGGvfi:VF_1964.
PATRIC20114620. VBIVibFis127983_1991.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05007.

Enzyme and pathway databases

BioCycAFIS312309:GIWP-2066-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]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
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_VIBF1
AccessionPrimary (citable) accession number: Q9XC07
Secondary accession number(s): Q5E3D7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 90 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