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Q9KPV0

- GLND_VIBCH

UniProt

Q9KPV0 - GLND_VIBCH

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 3 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 assimilation and metabolism.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.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: TIGR
  2. amino acid binding Source: InterPro
  3. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glutamine biosynthetic process Source: TIGR
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

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
Ordered Locus Names:VC_2262
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 876876Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192771Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243277.VC2262.

Structurei

3D structure databases

ProteinModelPortaliQ9KPV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 584134HDUniRule annotationAdd
BLAST
Domaini693 – 77785ACT 1UniRule annotationAdd
BLAST
Domaini800 – 87677ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 332332UridylyltransferaseAdd
BLAST
Regioni333 – 692360Uridylyl-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

Phylogenomic databases

eggNOGiCOG2844.
KOiK00990.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.

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. 1 hit.
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.

Q9KPV0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPYQSPITFQ EPQLTVESLK QQLESFTEYQ KQEFFDHHPV TDLVLGRSEY
60 70 80 90 100
MDLLLHRLWQ FFGFDELVEV SLVAVGGYGR GELHPLSDID LLVLSQQPLS
110 120 130 140 150
EQVANKISQF LTLLWDLKLE IGHAVRTVEQ CAEIGKADLT VATNLQEARL
160 170 180 190 200
LCGCEETFHR LKMVIHSESF WPSEIFYQAK VREQKERHAR YHDTTYNLEP
210 220 230 240 250
DIKSTPGGLR DIHTLSWVAR RHFGATSLYE MSRFGFLTDA EYRELVECQD
260 270 280 290 300
FLWRVRFALH IELKRYDNRL TFAHQVQVAR HLGYFGEGNR GIEMMMKEFF
310 320 330 340 350
RTLRRVAELN KMLLKIFDKA ILNNGEEAEA VIIDDDFQRR GNMIEARKPA
360 370 380 390 400
LFQARPETIL DMFLHMASDS TIESVAPATM RQLRTARRRL NKFLHTLPAA
410 420 430 440 450
REKFIELVRH PNALHKAFSQ MHKLGVLAAY LPQWNQIVGQ MQFDLFHVYT
460 470 480 490 500
VDEHSIRLLK HIHLFSDANN HDRHPICCEI YPKIQKKELL ILAAIFHDIG
510 520 530 540 550
KGRGGDHSEI GADEAFDFCI EHGLSKPEAK LVAWLVKNHL LMSVTAQRRD
560 570 580 590 600
IYDPDVIIEF AKKVRDEERL EYLVCLTVAD ICATNPELWN SWKRTLLAEL
610 620 630 640 650
FYSTQRALRR GLENPVDVRE RIRHNQQMAS ALLRKEGFSS REIEVLWQRF
660 670 680 690 700
KADYFLRHTH KQIAWHCTHL LRHEDSSKPL VLLSKKATRG GTEVFIYTKD
710 720 730 740 750
QAALFATVVA ELDRRNLNVH DAQIMASKDG YVLDTFMVLD QNGQAIEEDR
760 770 780 790 800
HQALIRHLVH VLEDGRPTTQ KARRIPRNLQ HFKVKTQVDF LPTKSKKRTL
810 820 830 840 850
MEFVALDTPG LLATVGATFA ELNLDLHAAK ITTIGERAED LFILTNAQGT
860 870
RLNEEEEQHL REKLIEHVAE LAPSAQ
Length:876
Mass (Da):101,542
Last modified:July 5, 2004 - v2
Checksum:iD7A48AB39C755C32
GO

Sequence cautioni

The sequence AAF95406.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF95406.1. Different initiation.
PIRiE82097.
RefSeqiNP_231893.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95406; AAF95406; VC_2262.
GeneIDi2613184.
KEGGivch:VC2262.
PATRICi20083567. VBIVibCho83274_2158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF95406.1 . Different initiation.
PIRi E82097.
RefSeqi NP_231893.1. NC_002505.1.

3D structure databases

ProteinModelPortali Q9KPV0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC2262.

Protocols and materials databases

DNASUi 2613184.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF95406 ; AAF95406 ; VC_2262 .
GeneIDi 2613184.
KEGGi vch:VC2262.
PATRICi 20083567. VBIVibCho83274_2158.

Phylogenomic databases

eggNOGi COG2844.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

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. 1 hit.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiGLND_VIBCH
AccessioniPrimary (citable) accession number: Q9KPV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3