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Q53245 (GLND_RHITR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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
OrganismRhizobium tropici
Taxonomic identifier398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length948 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 caution

The sequence AAC32290.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 948948Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192761

Regions

Domain490 – 603114HD
Domain729 – 81082ACT 1
Domain840 – 92182ACT 2
Region1 – 372372Uridylyltransferase HAMAP-Rule MF_00277
Region373 – 728356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q53245 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 9CCE1A43545213BD

FASTA948106,423
        10         20         30         40         50         60 
METHHIDFST VLDVSALKAE CEALAKRGLD KNEERSALLA LLKKASQDGR EEARRLLIAD 

        70         80         90        100        110        120 
GSGLNCAHRI SWLQDQIITV LYDLTVHHAY PKQAGVFSVT AVGGYGRDTL APGSDIDLLF 

       130        140        150        160        170        180 
LFQPKPASET HKAVEFILYM LWDMGFKVGH ATRSVEECIR EAKSDMTVRT AILETRYICG 

       190        200        210        220        230        240 
NVALERELQA RFDKEIVTNT GPEFIAAKLA ERDERHRKAG DTRYLVEPNV KEGKGGLRDL 

       250        260        270        280        290        300 
HTLFWISKYY YHVRDPAELV KLGVLSKQEY RLFEKAEDFL WAVRCHMHFL TGKAEERLSF 

       310        320        330        340        350        360 
DIQRDIAAAL DYNARPGLSA VERFMKHYFL VAKDVGDLTR ILCAALEDQQ AKATPGLTGV 

       370        380        390        400        410        420 
ISRFANRSRK IPGTVEFVED RGRIALANPD VFKRDPVSLI RLFFVADING LEFHPDALKR 

       430        440        450        460        470        480 
VTRSLSLIDN DLRENEEANR LFLSILTSKR DPALILRRMN EAGVLGRFIP EFGKIVSMMQ 

       490        500        510        520        530        540 
FNMYHHYTVD EHLIRAVEVL SEIDKGRAED IHPLTNKLMP NIEDRDALYV AVLLHDIAKG 

       550        560        570        580        590        600 
REEDHSEAGA AVARKLCPRF GLSPKQTELV VWLIAEHLTM SMVAQTRDLT DRKTIIDFAD 

       610        620        630        640        650        660 
RVQSLDRLKM LLILTVCDIR AVGPGVWNGW KGQLLRTLYY ETELLLSGGF SEVSRKERAE 

       670        680        690        700        710        720 
AAAEALEHAL ADWSQKERKA YVKLHYQPYL LSVPLEDQIR HTQFMRESDK AGKVLATMVR 

       730        740        750        760        770        780 
TDSFHAITEI TVLSPDHPRL LTVIAGACAA AGANIADAQI FTTSDGRALD TIHVSREFPD 

       790        800        810        820        830        840 
DADELRRAAT IGKMIEDVLA GRKRLPEVIA TRTKNRRKNK AFVIPPSVII TNSLSNKFTV 

       850        860        870        880        890        900 
IEVECLDRPG LLSEITAVLS DLSLDIQSAR ITTFGEKVID TFYVADLVGQ KISNENRRAY 

       910        920        930        940 
ITARLKAVMA GEEDEMRERM PSGIIAPAAT RGVAVEKSDT EKKAGSAA 

« Hide

References

[1]O'Connell K.P., Raffel S.J., Saville B.J., Handelsman J.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CIAT899.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U47030 Genomic DNA. Translation: AAC32290.1. Different initiation.

3D structure databases

ProteinModelPortalQ53245.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 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_RHITR
AccessionPrimary (citable) accession number: Q53245
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 73 of the entry and version 2 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