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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 Inferred.1 Publication

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. metal ion binding Source: InterPro
  4. 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 enzyme
Short name:
UTase/UR
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein
Including the following 2 domains:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
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 enzymeUniRule annotationPRO_0000192739Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP41393.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini465 – 598134HDAdd
BLAST
Domaini706 – 78681ACT 1Add
BLAST
Domaini813 – 88775ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 346346UridylyltransferaseUniRule annotationAdd
BLAST
Regioni347 – 705359Uridylyl-removingUniRule annotationAdd
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 By similarity.UniRule annotation

Sequence similaritiesi

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

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

MSNSLSNTVP PDLSAQPENP GEWPKSDFNC ATIKALIDAF QRWLGEAFDS    50
GIAAERLIEA RTEFIDQLLQ RLWVEYGFGS INDIALVAVG GYGRGELHPL 100
SDIDLLILSR KKLPDEQAQK VGERLALLWD IKLEVGHSVR TLEECLLEGL 150
SDLSVATNLI ESRLLIGDVA LFLELQKHIF SDGFWPSEKF FAAKVEEQND 200
RHQRYHGTSY NLEPDVKSSP GGLRDIHTLQ WIARRHFGAT SLDEMVGFGF 250
LTEAERNELN ECLHQLWRIR FALHLELNRY DNRLLFDRQF SVARRLRYEG 300
ESNQPIEHMM KDFFRVTRRV SELNQMLIQL FEEAILALTE DEKPRPIDDD 350
FQLRGTLIDL RDDTLFIREP QAILRMFYTM VRNSSITGIY STTVRHLRHA 400
RRHLTQPLCY IPEARTLFLS MLRHQGGLSR GLLPMHRHSV LWAYMPQWSH 450
IVGQMQFDLF HAYTVDEHTI RVLLKLESFA KEETRSRHPL WLELWPRLTH 500
PELILIAALF HDIAKGAGGD HSILGAQDVL KFAELHGLNC AQTQLVAWLV 550
RHQLLMSVTA QRRDIQDPEV IKQFAEEVQT ENRLHYLVCL TVADICATNE 600
NLWNSWKQSL LRELYFATEK QLRRGMQNTP DMRERVRHHQ LQALALLRME 650
NINEQALHQI WNRCRANYFV RHTPNQLAWH ARNLLKHDLS KPMILLSSHA 700
TRGGTEIFIW SPDRPYLFAA VSAELDRRNL SVHDAQIFTT RDGMAMDTFI 750
VLEPDGSPLS ADRTQMIRVG LEQTLSQRSW QPPAPRRQAA KLRHFSVPTE 800
VNFLPTHTDR KSFLELIALD QPGLLARVGQ VFADLGISLH GARITTIGER 850
VEDLFIIATA DRRALNNELQ QEVQQRLTEA LNPNDKG 887
Length:887
Mass (Da):102,344
Last modified:November 1, 1995 - v1
Checksum:i73782E94DA434CAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78685 Genomic DNA. Translation: CAA55353.1.
PIRiS54756. S43196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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: June 11, 2014
This is version 74 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

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