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B0KS97 (GLND_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:PputGB1_1144
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [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_1000078808

Regions

Domain481 – 590110HD
Domain706 – 78479ACT 1
Domain816 – 90085ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B0KS97 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 7650D665F9A853D7

FASTA900102,573
        10         20         30         40         50         60 
MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRLAGEVLD KRFRAGSEIR PLIEARAWLV 

        70         80         90        100        110        120 
DNILQQAWNQ FDWGDQSGIA LVAVGGYGRG ELHPHSDIDL LILLGAAEHE QYRDAIERFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRTVDEC AEQARADLTV ITNLMESRTI CGPEALRQRM LEVTSTAHMW 

       190        200        210        220        230        240 
PSKEFFLAKR AELKARHHKY NDTEYNLEPN VKGSPGGLRD IQTVLWVARR QYGTLNLHAL 

       250        260        270        280        290        300 
AGEGFLLESE NELLASSQDF LWKVRYALHM LAGRAEDRLL FDHQRSLATL LGYGDDNPKR 

       310        320        330        340        350        360 
AIEQFMQQYY RVVMSISQLC DLIVQHFEEV ILADEESGST QPLNARFRLH DGYIEAANPN 

       370        380        390        400        410        420 
VFKRTPFAML EIFVLMAQRP EIKGVRADTV RLLREHRHLI DDTFRTDIRN TSLFIELFKC 

       430        440        450        460        470        480 
EIGIHRNLRR MNRYGILGRY LPEFGLIVGQ MQHDLFHIYT VDAHTLNLIK HLRKLQYTPV 

       490        500        510        520        530        540 
SEKFPLASKL MGRLPKPELI YLAGLYHDIG KGRQGDHSEI GAVDAQKFCE RHQLPAWDSR 

       550        560        570        580        590        600 
LIVWLVQNHL VMSTTAQRKD LSDPQVINDF ALHVGDETRL DYLYVLTVAD INATNPSLWN 

       610        620        630        640        650        660 
SWRASLLRQL YTETKRALRR GLENPLDREE QIRQTQSSAL DILVREGTDP DDVEQLWSQL 

       670        680        690        700        710        720 
GDDYFLKHNA ADVAWHTDAI LQQPADGGPL VLIKETTQRE FEGGTQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMSQLNL NIHDARIITS SSQFTLDTYI VLDNDGGSIG DNPQRVKQIR DGLTEALRNP 

       790        800        810        820        830        840 
EDYPTIIQRR VPRQLKHFDF PPQVTILNDA QRPVTILEIT APDRPGLLAR LGRIFLEFDL 

       850        860        870        880        890        900 
SLQNAKIATL GERVEDVFFI TDADNQPLSD PQLCSRLQEA IVQQLQAGQG SDTSPTRVTF 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABY97052.1.
RefSeqYP_001667388.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KS97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_1144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY97052; ABY97052; PputGB1_1144.
GeneID5868903.
KEGGppg:PputGB1_1144.
PATRIC19929261. VBIPsePut76638_1150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-1174-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]
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_PSEPG
AccessionPrimary (citable) accession number: B0KS97
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: June 11, 2014
This is version 46 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