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Q4KHH8 (GLND_PSEF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:PFL_1174
OrganismPseudomonas fluorescens (strain Pf-5 / ATCC BAA-477) [Complete proteome] [HAMAP]
Taxonomic identifier220664 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length900 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 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192753

Regions

Domain481 – 57696HD
Domain706 – 78984ACT 1
Domain816 – 89580ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q4KHH8 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 40F0D6C35069651E

FASTA900103,314
        10         20         30         40         50         60 
MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRQAREVLD TRFRSGREIR RLIEDRAWFI 

        70         80         90        100        110        120 
DNILQKAWDQ FSWSEDADIA LVAVGGYGRG ELHPYSDIDL LILLDSADHE IFRDSIERFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRSVDEC AEQARADLTV ITNLMESRTI AGPEHLRQRM LQVTSTEHMW 

       190        200        210        220        230        240 
PSKDFFLAKR AEQKARHHKY NDTEYNLEPN VKGSPGGLRD IQTILWVARR QYGTLNLRAL 

       250        260        270        280        290        300 
AGEGFLVESE NALLASSQEF LWKVRYALHM LAGRAEDRLL LDHQRSIATL LGFEGEDAKQ 

       310        320        330        340        350        360 
SIESFMQQYY RVVMSIAQLS DLIIQHFEEV ILAPEDEAPP QPINARFQLH DGYIEAINDN 

       370        380        390        400        410        420 
VFKRTPFAML EIFVLMAQHP EIKGVRADTI RLLREHRHLI DDDFRHDIRN TSLFIELFKC 

       430        440        450        460        470        480 
EIGIHRNLRR MNRYGILGRY LPEFGFIVGQ MQHDLFHIYT VDAHTLNLIK HLRKMQYTPI 

       490        500        510        520        530        540 
SEKFPLASKL MGKLPKPELI YLAGLYHDIG KGRHGDHSEI GAVDAEAFCV RHQLPQWDTR 

       550        560        570        580        590        600 
LIVWLVQNHL VMSTTAQRKD LSDPQVIHDF AQIVVDQTRL DYLYVLTVAD IYATNPTLWN 

       610        620        630        640        650        660 
SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQSAAL DILVRNGTDP DEVEQLWSQL 

       670        680        690        700        710        720 
GDDYFLRHTA GDVAWHSDAI LQQPADGGPL VLIKEITQRE FEGGTQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMDQLNL NIHDARIITS SSQFTLDTYI VLDNDGESIG NNPQRVEQIR KGLTDALRNP 

       790        800        810        820        830        840 
DDYPTIIQRR VPRQLKHFAF APEVTIHNDA QRPVTVLELS APDRPGLLAR IGKIFLEFDL 

       850        860        870        880        890        900 
SLQNAKIATL GERVEDVFFI TDAHNQPLSD PQLCSRLQDA IVEQLSVSHE PTIEMTRLSI 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000076 Genomic DNA. Translation: AAY90461.1.
RefSeqYP_258305.1. NC_004129.6.

3D structure databases

ProteinModelPortalQ4KHH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220664.PFL_1174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY90461; AAY90461; PFL_1174.
GeneID3478991.
KEGGpfl:PFL_1174.
PATRIC19871555. VBIPseFlu72549_1206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK00275.

Enzyme and pathway databases

BioCycPFLU220664:GIX8-1178-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_PSEF5
AccessionPrimary (citable) accession number: Q4KHH8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 63 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