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P41393 (GLND_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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
OrganismKlebsiella oxytoca
Taxonomic identifier571 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length887 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 fixation and metabolism Probable. Ref.1

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

Disruption phenotype

Cells lacking this gene are unable to uridylylate PII and are altered in adenylation/deadenylation of glutamine synthetase. Ref.1

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 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192739

Regions

Domain465 – 598134HD
Domain706 – 78681ACT 1
Domain813 – 88775ACT 2
Region1 – 346346Uridylyltransferase HAMAP-Rule MF_00277
Region347 – 705359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
P41393 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 73782E94DA434CAC

FASTA887102,344
        10         20         30         40         50         60 
MSNSLSNTVP PDLSAQPENP GEWPKSDFNC ATIKALIDAF QRWLGEAFDS GIAAERLIEA 

        70         80         90        100        110        120 
RTEFIDQLLQ RLWVEYGFGS INDIALVAVG GYGRGELHPL SDIDLLILSR KKLPDEQAQK 

       130        140        150        160        170        180 
VGERLALLWD IKLEVGHSVR TLEECLLEGL SDLSVATNLI ESRLLIGDVA LFLELQKHIF 

       190        200        210        220        230        240 
SDGFWPSEKF FAAKVEEQND RHQRYHGTSY NLEPDVKSSP GGLRDIHTLQ WIARRHFGAT 

       250        260        270        280        290        300 
SLDEMVGFGF LTEAERNELN ECLHQLWRIR FALHLELNRY DNRLLFDRQF SVARRLRYEG 

       310        320        330        340        350        360 
ESNQPIEHMM KDFFRVTRRV SELNQMLIQL FEEAILALTE DEKPRPIDDD FQLRGTLIDL 

       370        380        390        400        410        420 
RDDTLFIREP QAILRMFYTM VRNSSITGIY STTVRHLRHA RRHLTQPLCY IPEARTLFLS 

       430        440        450        460        470        480 
MLRHQGGLSR GLLPMHRHSV LWAYMPQWSH IVGQMQFDLF HAYTVDEHTI RVLLKLESFA 

       490        500        510        520        530        540 
KEETRSRHPL WLELWPRLTH PELILIAALF HDIAKGAGGD HSILGAQDVL KFAELHGLNC 

       550        560        570        580        590        600 
AQTQLVAWLV RHQLLMSVTA QRRDIQDPEV IKQFAEEVQT ENRLHYLVCL TVADICATNE 

       610        620        630        640        650        660 
NLWNSWKQSL LRELYFATEK QLRRGMQNTP DMRERVRHHQ LQALALLRME NINEQALHQI 

       670        680        690        700        710        720 
WNRCRANYFV RHTPNQLAWH ARNLLKHDLS KPMILLSSHA TRGGTEIFIW SPDRPYLFAA 

       730        740        750        760        770        780 
VSAELDRRNL SVHDAQIFTT RDGMAMDTFI VLEPDGSPLS ADRTQMIRVG LEQTLSQRSW 

       790        800        810        820        830        840 
QPPAPRRQAA KLRHFSVPTE VNFLPTHTDR KSFLELIALD QPGLLARVGQ VFADLGISLH 

       850        860        870        880 
GARITTIGER VEDLFIIATA DRRALNNELQ QEVQQRLTEA LNPNDKG 

« Hide

References

[1]"The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation."
Edwards R.A., Merrick M.J.
Mol. Gen. Genet. 247:189-198(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
Strain: M5a1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78685 Genomic DNA. Translation: CAA55353.1.
PIRS43196. S54756.

3D structure databases

ProteinModelPortalP41393.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 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_KLEOX
AccessionPrimary (citable) accession number: P41393
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 74 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