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A6U5G1 (GLND_SINMW) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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:Smed_0031
OrganismSinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]
Taxonomic identifier366394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length949 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 fixation 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 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022354

Regions

Domain494 – 608115HD
Domain734 – 81582ACT 1
Domain845 – 92682ACT 2
Region1 – 377377Uridylyltransferase HAMAP-Rule MF_00277
Region378 – 733356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A6U5G1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: E18E0283457CC20C

FASTA949106,228
        10         20         30         40         50         60 
MARHETSFPE ILDVAALRAR CDFIASAHAE QREPMRRALL AAFKEANIAG RAKARELLAA 

        70         80         90        100        110        120 
DGAGIKCAER ISWLQDQLIT LLHDFVLNQV FDAAKAPETS RIAVTAVGGY GRGTLAPGSD 

       130        140        150        160        170        180 
IDLLFLLPAK KAVWAEPAIE FMLYILWDLG FKVGHATRTI EDCIRLSRAD MTIRTAILEC 

       190        200        210        220        230        240 
RYVCGSVALA SELETRFDHE IVRNTGPEFI AAKLAERDER HRKAGDTRYL VEPNVKEGKG 

       250        260        270        280        290        300 
GLRDLHTLFW ISKYFYRVKD SADLVKLGVL SRQEYKLFQK AEDFLWAVRC HMHFLTGKAE 

       310        320        330        340        350        360 
ERLSFDIQRE IAEALGYHDH PGLSAVERFM KHYFLVAKDV GDLTRIFCSA LEDQQAKDAP 

       370        380        390        400        410        420 
GISGVISRFR NRVRKIPGTL DFVDDGGRIA LASPDVFKRD PVNLLRMFHI ADINGLEFHP 

       430        440        450        460        470        480 
AALKQVTRSL SLITPHLREN EEANRLFLSI LTSRRNPELI LRRMNEAAVL GRFIPEFGKI 

       490        500        510        520        530        540 
VSMMQFNMYH HYTVDEHLLR AVDVLSRIER GLEEEAHPLT AMLMPAIEDR EALYVAVLLH 

       550        560        570        580        590        600 
DIAKGRPEDH SVAGAKVARK LCPRFRLSPK QTETVVWLVE EHLTMSMVAQ TRDLNDRKTI 

       610        620        630        640        650        660 
VDFAERVQSL ERLKMLLILT VCDIRAVGPG VWNGWKGQLL RTLYYETELL LSGGFSELSR 

       670        680        690        700        710        720 
KERAKHAADM LEEALADWPK EERQTYVRLH YQPYLLTVAL DEQVRHAAFI READAAGRTL 

       730        740        750        760        770        780 
ATMVRTHDFH AITEITVLSP DHPRLLTVIA GACAAAGANI VGAQIHTTSD GRALDTILVN 

       790        800        810        820        830        840 
REFSVAEDET RRAASIGKLI EDVLSGRKKL PDVIASRTRS KKRSRAFTVT PEVTISNALS 

       850        860        870        880        890        900 
NKFTVIEVEG LDRTGLLSEV TAVLSDLSLD IASAHITTFG EKVIDTFYVT DLVGSKITSE 

       910        920        930        940 
NRQMNIAARL KAVLAGEVDE ARERMPSGII APTPVPRASH GSKATKAET 

« Hide

References

[1]"Complete sequence of Sinorhizobium medicae WSM419 chromosome."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000738 Genomic DNA. Translation: ABR58891.1.
RefSeqYP_001325726.1. NC_009636.1.

3D structure databases

ProteinModelPortalA6U5G1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING366394.Smed_0031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR58891; ABR58891; Smed_0031.
GeneID5320858.
KEGGsmd:Smed_0031.
PATRIC23618827. VBISinMed134228_3085.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycSMED366394:GJAL-31-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. 2 hits.
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_SINMW
AccessionPrimary (citable) accession number: A6U5G1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: June 11, 2014
This is version 55 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