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A5UBF9

- GLND_HAEIE

UniProt

A5UBF9 - GLND_HAEIE

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, CGSHiEE_03445
Organism
Haemophilus influenzae (strain PittEE)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity.UniRule annotation

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. metal ion binding Source: InterPro
  4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciHINF374930:GJDD-668-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
Ordered Locus Names:CGSHiEE_03445
OrganismiHaemophilus influenzae (strain PittEE)
Taxonomic identifieri374930 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000006555: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 863863Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000022344Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi374930.CGSHiEE_03445.

Structurei

3D structure databases

ProteinModelPortaliA5UBF9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini446 – 579134HDAdd
BLAST
Domaini688 – 77285ACT 1Add
BLAST
Domaini794 – 86370ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 328328UridylyltransferaseUniRule annotationAdd
BLAST
Regioni329 – 687359Uridylyl-removingUniRule annotationAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.
Contains 2 ACT domains.
Contains 1 HD domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5UBF9-1 [UniParc]FASTAAdd to Basket

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MLFPLSLSSP LTPSAVKIER ENLKQFELEN FSRYSIFELV ENRSDFYDAL    50
LIQLWQEMGL SEQLGISLIA VGGYGRREMF PLSDLDFLIL VEQTPIPEIE 100
EKITQFIQFL WDCGFEVGHS VRTLQQCESE GKQDITIATN LLEARFLIGN 150
RPHFDALNEL VKRADFWSKE GFFNAKVQEQ IERYQRYHNT AYNLEPDIKY 200
SPGGLRDLHL LYWVALHHSG AQTLEDILQS GFIYPQEYQQ LQESRAFLFK 250
VRFALHLILT RYDNRLLFDR QIKVSELLGF RGEGNQAVEK MMKCFFQALH 300
RISLISNLLI QHYRENVLSS NQATVIEQLD DDFQLINQCL CLRNSLVFQE 350
KPARILDLFF YLTQYEQANI HSDTLRQLQI SLEQLPQKLC EIPEAREKFL 400
RLFNQPNSIK RAFMPMHQYG VLTAYLPQWQ AIEGLMQFDL FHIYTVDEHT 450
LRVMLKLESF LSQESAQEHP IAHRIFSQLS DRTLLYIAAL FHDIAKGRGG 500
DHAELGAKDV ANFARLHGLD RREIDTLAWL VQSHLLMSIT AQRRDIHDPE 550
VVMNFAEAVQ NQVRLDYLTC LTVADICATN GNLWNSWKRS LFASLYEFTE 600
QQFAQGMKEL LDYSEKSAEN RKLAQQILTQ DYSDIMPISI DQLWERCPED 650
YFVRNTPKQI AWHTSLLVDL VEALLVKISN RFSLGGTEVF IYCQDQPHLF 700
NKVVSTIGAK KFSIHDAQII TTQDGYVFDS FIITELNGEL VEFDRRRELE 750
QALTLALQSE KLSALSITPN RQLQHFTVQT DVRFLHENKK EHTEMELVAL 800
DKAGLLAQVS QIFSELNLNL LNAKITTVGE KAEDFFILTN QFGQALDSQQ 850
REILRNVLYR NIG 863
Length:863
Mass (Da):100,197
Last modified:July 10, 2007 - v1
Checksum:iFBC5A42D0FFB0B92
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000671 Genomic DNA. Translation: ABQ98110.1.
RefSeqiYP_001290493.1. NC_009566.1.

Genome annotation databases

EnsemblBacteriaiABQ98110; ABQ98110; CGSHiEE_03445.
GeneIDi5225241.
KEGGihip:CGSHiEE_03445.
PATRICi20277493. VBIHaeInf81350_0696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000671 Genomic DNA. Translation: ABQ98110.1 .
RefSeqi YP_001290493.1. NC_009566.1.

3D structure databases

ProteinModelPortali A5UBF9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374930.CGSHiEE_03445.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ98110 ; ABQ98110 ; CGSHiEE_03445 .
GeneIDi 5225241.
KEGGi hip:CGSHiEE_03445.
PATRICi 20277493. VBIHaeInf81350_0696.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci HINF374930:GJDD-668-MONOMER.

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
    Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
    Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PittEE.

Entry informationi

Entry nameiGLND_HAEIE
AccessioniPrimary (citable) accession number: A5UBF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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