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P41393

- GLND_KLEOX

UniProt

P41393 - GLND_KLEOX

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Klebsiella oxytoca
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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).1 Publication

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen fixation Source: UniProtKB-KW
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
OrganismiKlebsiella oxytoca
Taxonomic identifieri571 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192739Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP41393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini465 – 598134HDUniRule annotationAdd
BLAST
Domaini706 – 78681ACT 1UniRule annotationAdd
BLAST
Domaini813 – 88775ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 346346UridylyltransferaseAdd
BLAST
Regioni347 – 705359Uridylyl-removingAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.UniRule annotation
Contains 2 ACT domains.UniRule annotation
Contains 1 HD domain.UniRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41393-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNSLSNTVP PDLSAQPENP GEWPKSDFNC ATIKALIDAF QRWLGEAFDS
60 70 80 90 100
GIAAERLIEA RTEFIDQLLQ RLWVEYGFGS INDIALVAVG GYGRGELHPL
110 120 130 140 150
SDIDLLILSR KKLPDEQAQK VGERLALLWD IKLEVGHSVR TLEECLLEGL
160 170 180 190 200
SDLSVATNLI ESRLLIGDVA LFLELQKHIF SDGFWPSEKF FAAKVEEQND
210 220 230 240 250
RHQRYHGTSY NLEPDVKSSP GGLRDIHTLQ WIARRHFGAT SLDEMVGFGF
260 270 280 290 300
LTEAERNELN ECLHQLWRIR FALHLELNRY DNRLLFDRQF SVARRLRYEG
310 320 330 340 350
ESNQPIEHMM KDFFRVTRRV SELNQMLIQL FEEAILALTE DEKPRPIDDD
360 370 380 390 400
FQLRGTLIDL RDDTLFIREP QAILRMFYTM VRNSSITGIY STTVRHLRHA
410 420 430 440 450
RRHLTQPLCY IPEARTLFLS MLRHQGGLSR GLLPMHRHSV LWAYMPQWSH
460 470 480 490 500
IVGQMQFDLF HAYTVDEHTI RVLLKLESFA KEETRSRHPL WLELWPRLTH
510 520 530 540 550
PELILIAALF HDIAKGAGGD HSILGAQDVL KFAELHGLNC AQTQLVAWLV
560 570 580 590 600
RHQLLMSVTA QRRDIQDPEV IKQFAEEVQT ENRLHYLVCL TVADICATNE
610 620 630 640 650
NLWNSWKQSL LRELYFATEK QLRRGMQNTP DMRERVRHHQ LQALALLRME
660 670 680 690 700
NINEQALHQI WNRCRANYFV RHTPNQLAWH ARNLLKHDLS KPMILLSSHA
710 720 730 740 750
TRGGTEIFIW SPDRPYLFAA VSAELDRRNL SVHDAQIFTT RDGMAMDTFI
760 770 780 790 800
VLEPDGSPLS ADRTQMIRVG LEQTLSQRSW QPPAPRRQAA KLRHFSVPTE
810 820 830 840 850
VNFLPTHTDR KSFLELIALD QPGLLARVGQ VFADLGISLH GARITTIGER
860 870 880
VEDLFIIATA DRRALNNELQ QEVQQRLTEA LNPNDKG
Length:887
Mass (Da):102,344
Last modified:November 1, 1995 - v1
Checksum:i73782E94DA434CAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78685 Genomic DNA. Translation: CAA55353.1.
PIRiS54756. S43196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78685 Genomic DNA. Translation: CAA55353.1 .
PIRi S54756. S43196.

3D structure databases

ProteinModelPortali P41393.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGLND_KLEOX
AccessioniPrimary (citable) accession number: P41393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3