Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A4XWU3

- GLND_PSEMY

UniProt

A4XWU3 - GLND_PSEMY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas mendocina (strain ymp)
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

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 compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciPMEN399739:GHR6-3114-MONOMER.

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:Pmen_3055
OrganismiPseudomonas mendocina (strain ymp)
Taxonomic identifieri399739 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000229: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 899899Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000059224Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi399739.Pmen_3055.

Structurei

3D structure databases

ProteinModelPortaliA4XWU3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini488 – 56881HDUniRule annotationAdd
BLAST
Domaini706 – 78479ACT 1UniRule annotationAdd
BLAST
Domaini816 – 89782ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342UridylyltransferaseAdd
BLAST
Regioni343 – 705363Uridylyl-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.
HOGENOMiHOG000261778.
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.

A4XWU3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQMDPELFD RGQFQAELAL KSSPIAAFKK AIRHAREVLD ARFKGGRDIR
60 70 80 90 100
RLVEDRAWFV DQILQEAWKR FAWSEDADIA LLAVGGYGRG ELHPYSDIDL
110 120 130 140 150
LILLDSSDHE IFREPIEGFL TLLWDIGLEV GQSVRSVDEC AEEARADLTV
160 170 180 190 200
ITNLMESRTI AGPEHLRQRM QQVTSSEQMW PSKHFYLAKR EERKARHAKY
210 220 230 240 250
NDTEYNLEPN VKGSPGGLRD IQTVLWVARR QFGTLNLQAL VGQGFLLESE
260 270 280 290 300
YALLSSSQEF LWKVRYALHM LAGRAEDRLL FDYQARIAAL FGYQDGDGKR
310 320 330 340 350
SIEHFMQKYY RVVMGISELS DLINQHFEEV ILRAGESGPA TPLNSRFQVR
360 370 380 390 400
DGYIEVTHPN VFKRTPFAIL EVFVLMAQNP EIKGVRADSI RLLRDSRHLI
410 420 430 440 450
DDDFRKDIRN TSLFIELFKC KEGIHRNLRR MNRYGILGRY LPEFGHIVGQ
460 470 480 490 500
MQHDLFHIYT VDAHTLNLIK HLRKFRWPEL AEKFPLASKL IDRLPKPELI
510 520 530 540 550
YLAGLYHDIG KGRGGDHSEL GAVDAEAFAR RHQLPAWDSA LIVWLVQHHL
560 570 580 590 600
VMSTTAQRKD LSDPQVIHDF AQFVGDQTHL DYLYVLTVAD INATNPSLWN
610 620 630 640 650
SWRASLLRQL YTETKRALRR GLENPLDREE QIRQTQSAAL DILVRGGTDP
660 670 680 690 700
DDAEQLWSQL GDDYFLRHTA NDVAWHTEAI LQHPADSGPL VLIKETTQRE
710 720 730 740 750
FEGGTQIFIY APDQHDFFAV TVAAMSQLNL NIHDARIITS TSQFTLDTYV
760 770 780 790 800
VLDADGGSIG DNPARIKQIR EGLIEALKNP DEYPTIIQRR VPRQLKHFAF
810 820 830 840 850
APQVTIHNDA QRPVTILELT APDRPGLLAR IGRIFLEYDL SLQNAKIATL
860 870 880 890
GERVEDVFFV TDANNQPLSD PELCARLQET IVRRLSEPSA QPQSLQIDI
Length:899
Mass (Da):102,887
Last modified:May 29, 2007 - v1
Checksum:i6154CE68B882E4DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000680 Genomic DNA. Translation: ABP85809.1.
RefSeqiYP_001188541.1. NC_009439.1.

Genome annotation databases

EnsemblBacteriaiABP85809; ABP85809; Pmen_3055.
GeneIDi5107535.
KEGGipmy:Pmen_3055.
PATRICi19912722. VBIPseMen131592_3101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000680 Genomic DNA. Translation: ABP85809.1 .
RefSeqi YP_001188541.1. NC_009439.1.

3D structure databases

ProteinModelPortali A4XWU3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 399739.Pmen_3055.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP85809 ; ABP85809 ; Pmen_3055 .
GeneIDi 5107535.
KEGGi pmy:Pmen_3055.
PATRICi 19912722. VBIPseMen131592_3101.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci PMEN399739:GHR6-3114-MONOMER.

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: ymp.

Entry informationi

Entry nameiGLND_PSEMY
AccessioniPrimary (citable) accession number: A4XWU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: November 26, 2014
This is version 58 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3