Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3KHB4 (GLND_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Ordered Locus Names:Pfl01_1099
OrganismPseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]
Taxonomic identifier205922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length900 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 assimilation and metabolism By similarity. HAMAP-Rule MF_00277

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

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 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231686

Regions

Domain486 – 590105HD
Domain706 – 78984ACT 1
Domain816 – 90085ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3KHB4 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: B21FDACD3FA1D1A0

FASTA900102,820
        10         20         30         40         50         60 
MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRQAREVLD ARFRAGRDIR RLIEDRAWFV 

        70         80         90        100        110        120 
DNILQKAWDQ FDWSEDADIA LVAVGGYGRG ELHPYSDIDL LILLDSADHE IFRDSIERFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRSVDEC AEEARADLTV VTNLMESRTI CGPERLRQRM LDVTSTAHMW 

       190        200        210        220        230        240 
PSKDFFLAKR AEQKARHHKY NDTEYNLEPN VKGSPGGLRD IQTILWVARR QYGTLNLRAL 

       250        260        270        280        290        300 
AGEGFLVESE NALLASSQEF LWKVRYALHM LAGRSEDRLL FDHQRTIAGL LGFEGDDAKQ 

       310        320        330        340        350        360 
AVENFMQQYF RVVMSIAQLS DLIIQHFEEV ILAPEDEAPP QPINSRFQLH DGYIEARNDN 

       370        380        390        400        410        420 
VFRRTPFAML EIFVLMAQQP EIKGVRADTI RLLRENRHLI DDNFRNDIRN TSLFIELFKC 

       430        440        450        460        470        480 
KIGIHRNLRR MNRYGILGRY LPEFGFIVGQ MQHDLFHIYT VDAHTLNLIK HLRKLQYTQV 

       490        500        510        520        530        540 
SEKFPLAAKL MAKLPKPELI YMAGLYHDIG KGRHGDHSEI GAVDAEAFCQ RHQLPVWDSR 

       550        560        570        580        590        600 
LIVWLVQNHL VMSTTAQRKD LSDPQVIHDF ALAVGDETRL DYLYVLTVAD INATNPTLWN 

       610        620        630        640        650        660 
SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQSAAL DILVRGGTDP DDVEQLWAQL 

       670        680        690        700        710        720 
GDDYFLRHTA GDVAWHTDAI LQQPADGGPL VLIKETTQRE FEGGTQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMDQLNL NIHDARVITS SSQFTLDTYI VLDTDGDSIG DNPVRVKQIR DGLTEALRNP 

       790        800        810        820        830        840 
ADYPTIIQRR VPRQLKHFAF APQVTIHNDA QRPVTVLELT APDRPGLLAR VGGIFLEFDL 

       850        860        870        880        890        900 
SLQNAKIATL GERVEDVFFI TDAHNQPLSD PLLCSRLQDA IVEQLSVNQE PDIKLSRISI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000094 Genomic DNA. Translation: ABA72842.1.
RefSeqYP_346831.1. NC_007492.2.

3D structure databases

ProteinModelPortalQ3KHB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205922.Pfl01_1099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA72842; ABA72842; Pfl01_1099.
GeneID3716504.
KEGGpfo:Pfl01_1099.
PATRIC19884289. VBIPseFlu44242_1121.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK00275.

Enzyme and pathway databases

BioCycPFLU205922:GJBD-1118-MONOMER.

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]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 1 hit.
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_PSEPF
AccessionPrimary (citable) accession number: Q3KHB4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 69 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