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Q65SZ8 (GLND_MANSM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:MS1305
OrganismMannheimia succiniciproducens (strain MBEL55E) [Complete proteome] [HAMAP]
Taxonomic identifier221988 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBasfia

Protein attributes

Sequence length875 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 – 875875Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192743

Regions

Domain461 – 594134HD
Domain700 – 78283ACT 1
Domain806 – 87570ACT 2
Region1 – 343343Uridylyltransferase HAMAP-Rule MF_00277
Region344 – 699356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q65SZ8 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: E69E48587C5D349A

FASTA875100,522
        10         20         30         40         50         60 
MIGHNNFIIQ SVILRFFMFQ SVEGLLTPGL IKQQKEQLKQ TELENFAQAD VNSLISHRTL 

        70         80         90        100        110        120 
FCDNFLIRLW RQFSLHEVTD LALIAVGGYG RREIFPLSDL DFLILTEQPM PADLAKKVEE 

       130        140        150        160        170        180 
FIQFVWDCGF DVGASVRTLE DCDSQGRADI TIATNLLESR LLTGNETLFD KLSSIVGRED 

       190        200        210        220        230        240 
FWPRKTFFEA KIQEKKQRYQ RYNNTSYNLE PDIKYNPGGL RDLHLIYWIA LRHSNALSLE 

       250        260        270        280        290        300 
EILQSGFIYP EEYAELERNQ QFLFKVRFAL HLILKRYDNR LLFDRQVKVS ELLGYQGEGN 

       310        320        330        340        350        360 
QGVETMMKAF FQSLQAISLA SDILAKHYKE HFVDENGEEE CQVLDDNFQM INNAIFLVRE 

       370        380        390        400        410        420 
DCFVQQPDTI LDLFSYLIIR PQAELHSSTL RLLHLALGQL NGYLSELPAA REKFLRLLTQ 

       430        440        450        460        470        480 
PRGIERALIP MHKYGVLTAY IPEWKGIEGL MQFDLFHIYT VDEHTMRVLA KLETFLSEET 

       490        500        510        520        530        540 
AEAHPLCVKL FPSLPDRALI YIAALFHDIA KGRGGNHADL GAVDVGRFAA QHGFDCREIE 

       550        560        570        580        590        600 
TMKWLVKQHL FMSVTAQRRD IHDPEVVMNF AAEVQNQVRL NYLVCLTVAD ICATNTTLWN 

       610        620        630        640        650        660 
SWKRSLFASL YQYTNQQFNQ GMDNLLDNQE QEEQNKALAL EILQSQGFTE DVQSLWKRCP 

       670        680        690        700        710        720 
GDYFLRNTPK ELAWHAVLLA GVETELLVKI SNRFSAGGTE VFIYCKDRPN LFLKVVAAIG 

       730        740        750        760        770        780 
NKKLSIHDAQ IITSLDGYAF DSFIVTELDG SLLKFDRRRV LEKAIINSLN SNELTKLQGS 

       790        800        810        820        830        840 
ENHKLQHFNV KTEVRFLNTE KTTHTEMELF TLDKAGLLAD VSLVFSELNL SIQNAKITTI 

       850        860        870 
GEKAQDFFIL TNAKGEALSE RERQSLSEKL QARLD 

« Hide

References

[1]"The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens."
Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J.
Nat. Biotechnol. 22:1275-1281(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBEL55E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016827 Genomic DNA. Translation: AAU37912.1.
RefSeqYP_088497.1. NC_006300.1.

3D structure databases

ProteinModelPortalQ65SZ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221988.MS1305.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU37912; AAU37912; MS1305.
GeneID3077152.
KEGGmsu:MS1305.
PATRIC22445929. VBIManSuc86752_1190.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK01759.

Enzyme and pathway databases

BioCycBMAN221988:GHGM-1346-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.
PfamPF08335. 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_MANSM
AccessionPrimary (citable) accession number: Q65SZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 62 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