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

F0L5E2 (F0L5E2_AGRSH) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 27. Feed History...

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

Names and origin

Protein namesRecommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277

Short name=UTase/UR HAMAP-Rule MF_00277
Alternative name(s):
Bifunctional [protein-PII] modification enzyme HAMAP-Rule MF_00277
Bifunctional nitrogen sensor protein HAMAP-Rule MF_00277
Gene names
Name:glnD HAMAP-Rule MF_00277 EMBL ADY63324.1
Ordered Locus Names:AGROH133_03522 EMBL ADY63324.1
OrganismAgrobacterium sp. (strain H13-3) (Rhizobium lupini (strain H13-3)) [Complete proteome] [HAMAP] EMBL ADY63324.1
Taxonomic identifier861208 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length942 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 SAAS SAAS002912

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277 SAAS SAAS002912

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277 SAAS SAAS002912

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. HAMAP-Rule MF_00277

Contains 1 HD domain. HAMAP-Rule MF_00277

Contains 2 ACT domains. HAMAP-Rule MF_00277

Contains ACT domains. SAAS SAAS002912

Contains HD domain. SAAS SAAS002912

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain523 – 60684HD By similarity HAMAP-Rule MF_00277
Domain730 – 81182ACT 1 By similarity HAMAP-Rule MF_00277
Domain841 – 92080ACT 2 By similarity HAMAP-Rule MF_00277
Region1 – 373373Uridylyltransferase By similarity HAMAP-Rule MF_00277
Region374 – 729356Uridylyl-removing By similarity HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
F0L5E2 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 9C1AC9C8AB73259B

FASTA942106,259
        10         20         30         40         50         60 
MAIKDLDFSE ILDVSALKRE CDIIFKNDGK RIADVRSDLL PIFRKASTEG REKARELLKS 

        70         80         90        100        110        120 
DGSGIDCARR ISWLQDRLIE ILYDLACQYV YPKDAPQIAV AAVGGYGRGT LAPGSDIDLL 

       130        140        150        160        170        180 
FLLPAKNTPD MHKAVEFVLY LLWDLGFKVG HATRTVDECV RLSKSDMTIR TAILEVRAIC 

       190        200        210        220        230        240 
GKKSLTDDLE KRFESEVVTG TGPEFIAAKL AERDQRHRKA GDTRYLVEPN VKEGKGGLRD 

       250        260        270        280        290        300 
LHTLFWIAKY YYHVRDTADL VKLGVLSKRE LRLFEKADDF LWAVRCQMHF ITNKAEERLS 

       310        320        330        340        350        360 
FDIQREIADA LGYQPRPGLS AVERFMKHYF LVAKDVGDLT RIVCAALEDR QAKDVPGLSG 

       370        380        390        400        410        420 
VLSRFAHRVR KIPGSVEFVE DRGRIALAKP DVFKNDPVNL IRLFHIADIN NLELHPDALR 

       430        440        450        460        470        480 
VVTRSLSLIN DGLRENEEAN RLFLAILTSR RDPALTLRRM NEAGVLGKFI PEFGKIVAMM 

       490        500        510        520        530        540 
QFNMYHHYTV DEHLIRSVGV LSEVDKGTAV DAHPLANQLM PGVEEREALY VAVLLHDVAK 

       550        560        570        580        590        600 
GRQEDHSIAG ARVARKLCQR FRLTGKQTEM VVWLIEQHLL MSMVAQTRDL HDRKTITDFA 

       610        620        630        640        650        660 
DKVQSMERLK MLLILTVCDI RAVGPGVWNG WKGQLLRSLY YETELLLSGG FSEVSRKERA 

       670        680        690        700        710        720 
HIARQALYDA LEDWGQKARR KYTKLHYEPY LLTVALEDQV RHTRFIREAD KQEKALSTMV 

       730        740        750        760        770        780 
RTHSFHAITE ITVLAPDHPR LLSIITGACA AAGANIADAQ IFTTSDGRAL DTILINREFP 

       790        800        810        820        830        840 
IDEDETRRGN NVGKLIEEVL SGRQRLPEMI ATRTKSRRKK SAFTIPPSVI ISNGLSNKFT 

       850        860        870        880        890        900 
VIEVECLDRP GLLADMTAVI ADLSLDIHSA RITTFGEKVI DTFYVTDLFG QKVTNDNRQA 

       910        920        930        940 
SIATRLKAVM SEQEDELRDR MPNGIIAHPD VAALPATRTA KA 

« Hide

References

[1]"Complete genome sequencing of Agrobacterium sp. H13-3, the former Rhizobium lupini H13-3, reveals a tripartite genome consisting of a circular and a linear chromosome and an accessory plasmid but lacking a tumor-inducing Ti-plasmid."
Wibberg D., Blom J., Jaenicke S., Kollin F., Rupp O., Scharf B., Schneiker-Bekel S., Sczcepanowski R., Goesmann A., Setubal J.C., Schmitt R., Puhler A., Schluter A.
J. Biotechnol. 155:50-62(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H13-3 EMBL ADY63324.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002248 Genomic DNA. Translation: ADY63324.1.
RefSeqYP_004277644.1. NC_015183.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY63324; ADY63324; AGROH133_03522.
GeneID10266091.
KEGGagr:AGROH133_03522.
PATRIC46845387. VBIAgrSp164909_0335.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00990.
OMALYCLWDM.

Enzyme and pathway databases

BioCycASP861208:GH59-335-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 nameF0L5E2_AGRSH
AccessionPrimary (citable) accession number: F0L5E2
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 14, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)