Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6FAM5 (GLND_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:ACIAD2079
OrganismAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length888 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 – 888888Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192713

Regions

Domain491 – 58696HD
Domain700 – 78182ACT 1
Domain809 – 88779ACT 2
Region1 – 338338Uridylyltransferase HAMAP-Rule MF_00277
Region339 – 699361Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q6FAM5 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 1F244D77538E36FC

FASTA888102,208
        10         20         30         40         50         60 
MIITSPLLDY VTSHQDIKAI NQWRADVEQQ LQEFYENGYS IRDIVLARSN LIDEALTFLW 

        70         80         90        100        110        120 
KHAGLDQSDL GLFAVGGYGR REMLPYSDVD IMILSENDIS PEHEKQISGF ISSLWDVGNF 

       130        140        150        160        170        180 
KPGTSVRSIQ NCVEQATNDL TVATTLIESR LITGNPDLAK WPRRIVSQTW TDKTFFDAKM 

       190        200        210        220        230        240 
EEQAKRHAQH NNTESNLEPD IKNAPGGIRD MNQIGWIAKR HFRVNRIYDL VHLGFITEYE 

       250        260        270        280        290        300 
LKVLEEAESF LWEIRHHLHL LSKRDENRLL FDHQREIAAK FGYTRAEGQP VNFAVEQFMK 

       310        320        330        340        350        360 
RYYRTAQQVS TLNEMLLAYF NESVITPRLP NYERKIEEIN ENFKLVDGKL AVQHHKVFSE 

       370        380        390        400        410        420 
NPSAILELFY LLANHPEIEG IRARTLRLLI MAAKRIDQEF RDNPAHQALF MAIIRSPYRL 

       430        440        450        460        470        480 
YDTLVDMKRY GILGNYIPAF GQIMGLMQYD LFHIYTVDAH TLLLIRNLNR FKEPEFAQHF 

       490        500        510        520        530        540 
PVVSSVFQRL ARRDIVYLAA IFHDIAKGRG GDHSELGAED AIEFCRAHGF TERECKLVAW 

       550        560        570        580        590        600 
LIHNHLLMSL TAQKKDISDP DVIKEFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 

       610        620        630        640        650        660 
SLMRQLYTYS RDVIRSGLGR PVDYQMLIED TKFSASETLV NEFSLDAVEK VWQELGDEYF 

       670        680        690        700        710        720 
LKESADEIAW HTRAILQHGD NPAPIVLLRA HRQSAQDAVQ IFIYTQDKPN LFATTVAVLD 

       730        740        750        760        770        780 
RMNLDVQDAR IITATKAFSL DTYVVLDRFG TLLTDPEREH TVKEALIKAL SQSDKYPGLM 

       790        800        810        820        830        840 
QRRIPRQLRH FDIENTVDIT LNPVLQQNMV EISTLDQPGL LARVGGLFMM QGLDIHSAKI 

       850        860        870        880 
ATLGERAEDI FFVTKKDGQP MTTDEAHIFS AQLKLALDEA SNQIVSQH 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33305 / BD413 / ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG68888.1.
RefSeqYP_046710.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6FAM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING62977.ACIAD2079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG68888; CAG68888; ACIAD2079.
GeneID2881141.
KEGGaci:ACIAD2079.
PATRIC20741848. VBIAciSp98416_1868.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycASP62977:GJVV-1960-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. 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_ACIAD
AccessionPrimary (citable) accession number: Q6FAM5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 19, 2004
Last modified: June 11, 2014
This is version 71 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