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B4RC79 (GLND_PHEZH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:PHZ_c3463
OrganismPhenylobacterium zucineum (strain HLK1) [Complete proteome] [HAMAP]
Taxonomic identifier450851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

Protein attributes

Sequence length938 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 – 938938Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000114757

Regions

Domain496 – 624129HD
Domain734 – 81380ACT 1
Domain845 – 92480ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 733354Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B4RC79 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 4D684D54FEEEB95E

FASTA938102,982
        10         20         30         40         50         60 
MPPRLRPTHL EYVVDGVKLR SQLSAAALEH AGDELAQRRA ALEILKNALF RGRMIAKERL 

        70         80         90        100        110        120 
ENGAGGIETA RLLSGVTDEV VSALYDFTTV HVFRARNPTE GERLALMAVG GYGRGTLAPF 

       130        140        150        160        170        180 
SDIDLLFVRP YKQTAHAESV IEYMLYALWD LGFKVGHASR TIDECLKLSR EDFTIRTSIL 

       190        200        210        220        230        240 
EARRLTGDEK LAGELVERFR KEVVKGTGAE FVAAKLKERD ERHARAGASR YMVEPNVKEG 

       250        260        270        280        290        300 
KGGLRDLNTL FWIAQYLHPG ESLEKVMHLE IFDRREVRTF IQALDFLWAV RCHLHFATGR 

       310        320        330        340        350        360 
PEERLSFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLFAK DVGSLTRVFA AKLEADRVKT 

       370        380        390        400        410        420 
APKGISRFIP GRAQKRKPLD EPGFHEVGGR LGVDPEIFEA DPVNLLKLFR IADQRNLDLH 

       430        440        450        460        470        480 
PDAFTAASRA SGLITSAVRR DRHAAKVFLD ILARGRDPQR TLALMNEAGV LGRFVPEFGR 

       490        500        510        520        530        540 
IVAQMQFNMY HSYTVDEHTL RAVGVIADIA AGRLAEDHPL AVQTMPLIAD REALFLAMLL 

       550        560        570        580        590        600 
HDTGKGGAGG QELAGARAAR QACERLGLER SKIELVAWLV EHHLVMSDYA QKRDVSDPRT 

       610        620        630        640        650        660 
VADFARIVQS PERLRLLLVL TVADIRAVGP GVWNGWKGQL MRELYTATEA VFRGGRGSDA 

       670        680        690        700        710        720 
AAALKRYQEN AAYDARVSLA KADPLAEPWA DAMEDAYFTA FSEAEVLAHA RLAQQAGGGA 

       730        740        750        760        770        780 
AAEGRIRSEL NAAEVVVAAA DRPRLFVDLA EAITAAGANV MGARVFTSRA GQALDVFYVQ 

       790        800        810        820        830        840 
DASGQPFGSH DPRALARLAE TLACAARGEP VAREPRKPQD LGRTAAFAIT PAVMLDNEAS 

       850        860        870        880        890        900 
ETSTVVEASG RDRPGLLAAL ARTISDAGLS ILSAHIDGYG ERAVDAFYVV DADGRKLTDA 

       910        920        930 
RKRNALKSAL LAALTKAEAE TAQARRTNLQ RARASVAR 

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References

[1]"Complete genome of Phenylobacterium zucineum - a novel facultative intracellular bacterium isolated from human erythroleukemia cell line K562."
Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.
BMC Genomics 9:386-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000747 Genomic DNA. Translation: ACG79872.1.
RefSeqYP_002132301.1. NC_011144.1.

3D structure databases

ProteinModelPortalB4RC79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING450851.PHZ_c3463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG79872; ACG79872; PHZ_c3463.
GeneID6789416.
KEGGpzu:PHZ_c3463.
PATRIC22930318. VBIPheZuc44517_4213.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05092.

Enzyme and pathway databases

BioCycPZUC450851:GHUG-3508-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_PHEZH
AccessionPrimary (citable) accession number: B4RC79
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 41 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