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B8GWX0 (GLND_CAUCN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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:CCNA_00013
OrganismCaulobacter crescentus (strain NA1000 / CB15N) [Complete proteome] [HAMAP]
Taxonomic identifier565050 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length940 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 – 940940Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000132527

Regions

Domain497 – 627131HD
Domain737 – 82185ACT 1
Domain848 – 92982ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 736357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B8GWX0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 2F1985420353F8ED

FASTA940103,396
        10         20         30         40         50         60 
MPRRLRPTRL EHVVDGHALR ARLSAAALDS IGNEAEQRAR AIDILKQALF RGRMIAKERL 

        70         80         90        100        110        120 
ENGASGVETS RLLSGVTDEV ITALYDFTTV HVFRARNPTE GERLCLLAVG GYGRGTLAPF 

       130        140        150        160        170        180 
SDIDLLFLRP YKQTPHAESV IEYMLYALWD LGFKVGHASR TIEECVRLSK EDFTIRTSIL 

       190        200        210        220        230        240 
EARRLTGDER LAEDLKKRFR DEVMKATGAQ FVAAKLKERD DRQARAGASR YMVEPNVKEG 

       250        260        270        280        290        300 
KGGLRDLHTL MWIAEYLHPV DRPEDVFKME VFSIRETKAF IRAFDFLHAV RAHLHFTTGR 

       310        320        330        340        350        360 
PEERLTFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLIAK EVGTLTRAFS AKLEAEHFKN 

       370        380        390        400        410        420 
EPKGISRFLP GARPKRKALD VEGFYEDGGR LNIEGQEIFE ADPVNLIRLF KIADERDLDL 

       430        440        450        460        470        480 
HPDAFTAVTR ALPLITSRVR RDPDACRAFL DLLARGKRSY RTLTLMNDAG VLGRFIPEFG 

       490        500        510        520        530        540 
RVVAQMQFNM YHSYTVDEHT LRAVGVIGDI AAGRLVDDHP LAVSIMPLIE DREALFLAML 

       550        560        570        580        590        600 
LHDTGKGGVG GQEKAGARSA RSACERLGVE RSKVELVAWL VENHLVMSDF AQKRDVSDPG 

       610        620        630        640        650        660 
TVAAFARIVE NPERLRLLLV ITVADIRAVG PGVWNGWKGQ LLRELYNATE AVFRGGRGSD 

       670        680        690        700        710        720 
AAANVQRHQE STAEAARAAL LETDPAAKGW VAAMENAYFS AFSQDDLFHH AELARRAAIQ 

       730        740        750        760        770        780 
GGAAAEGQVR PGSNAAEVVI AAKDRRGLFA DLALAISSLG GNVVGARVFT SRQGQALDVF 

       790        800        810        820        830        840 
YVQDVTGAPF GCENPRALRR LADALEAAGK GDALAVEPRR GSEQTRAAAF AIAPSVTIDN 

       850        860        870        880        890        900 
DASNDATVVE ASGRDRPGLL HALAKTLADS ALSIQSAHID GYGERAVDAF YVQTTEGGKV 

       910        920        930        940 
TDTRKLNALK ADLLAALEQN EASAPAARPG LRRARASVAR 

« Hide

References

[1]"The genetic basis of laboratory adaptation in Caulobacter crescentus."
Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1000 / CB15N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001340 Genomic DNA. Translation: ACL93480.1.
RefSeqYP_002515388.1. NC_011916.1.

3D structure databases

ProteinModelPortalB8GWX0.
SMRB8GWX0. Positions 386-632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190650.CC_0013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL93480; ACL93480; CCNA_00013.
GeneID7332895.
KEGGccs:CCNA_00013.
PATRIC21304593. VBICauCre52860_0014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycCAULONA1000:CCNA_00013-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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_CAUCN
AccessionPrimary (citable) accession number: B8GWX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 42 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