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Q6D8E5

- GLND_PECAS

UniProt

Q6D8E5 - GLND_PECAS

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, ECA1029
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
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 fixation 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 fixation Source: UniProtKB-HAMAP
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciPATR218491:GJNB-1059-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:ECA1029
OrganismiPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Taxonomic identifieri218491 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
ProteomesiUP000007966: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 904904Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192731Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi218491.ECA1029.

Structurei

3D structure databases

ProteinModelPortaliQ6D8E5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini479 – 612134HD
Add
BLAST
Domaini720 – 80182ACT 1
Add
BLAST
Domaini827 – 90478ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 360360UridylyltransferaseUniRule annotation
Add
BLAST
Regioni361 – 719359Uridylyl-removingUniRule annotation
Add
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.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 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.

Q6D8E5-1 [UniParc]FASTAAdd to Basket

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MTDKRFSPDN TPPDASSPDS PIDTIAAAQP PVSPLTYADD MLNCQALKQQ    50
LELFQLWLGS EFRSGVSAEK LIDARTLFID RLLQRLWYCH GFENIAQTAL 100
VAVGGYGRGE LHPLSDIDVL VLSQTELSDE HSQRVGQFIT LLWDLKLEVG 150
HSVRTLEECL QEGRADISVA TNLIESRMIC GDVALFLTLQ KHVFSDEFWP 200
SPTFFPAKIT EQQERHQRYH STSYNLEPDI KSSPGGLRDI HTLLWVARRH 250
FGATSLNEMV GFGFLTEAER KELNECQSFL WRIRFALHLI LPRYDNRLLF 300
DRQLNVAQLL QYQGEGNTPV ERMMKDFYRM TRRVSELNQM LLQLFDEAIL 350
ALDASEKPRP IDDEFQLRGN LVDLRDENLF IKKPEAIMRM FYLMVRNRDI 400
SGIYSTTLRQ LRHARRHLAS PLCTIPEARQ LFMNILRHPY AVSRALLPMH 450
RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD EHTIRVLLKL ESFADEDTRP 500
QHPLCVELYP RLPQPELLLL AALFHDIAKG RGGDHSELGA LDVLEFAALH 550
GLNSREAQLV SWLVRCHLLM SVTAQRRDIQ DPTVIQQFAT EVQSETRLRY 600
LVSLTVADIC ATNETLWNSW KQSLLRELYF ATEKQLRRGM QNTPDLRERV 650
RHHRLQALAL LRMDNIDEEA LHHIWSRCRA DYFLRHSPNQ IAWHARHLLE 700
HDTNKPLVLI SHQASRGGTE IFIWSPDRPY LFAAVAGELD RRNLSVHDAQ 750
IFTSRDGMAM DTFIVLEPDG SPLAQDRHEM IRHALEQALT QRHYQHPRVR 800
RTSPKLRHFS VPTEVNFLPT HTDRRSYMEL SALDQPGLLA RIGEIFSDLN 850
LSLHGARIST IGERVEDLFI LADSDRRALK PELRLKLQER LTEALNPNDK 900
VPLS 904
Length:904
Mass (Da):104,412
Last modified:August 16, 2004 - v1
Checksum:i1A6A4DEF5361ED32
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950851 Genomic DNA. Translation: CAG73940.1.
RefSeqiYP_049136.1. NC_004547.2.

Genome annotation databases

EnsemblBacteriaiCAG73940; CAG73940; ECA1029.
GeneIDi2881763.
KEGGieca:ECA1029.
PATRICi20477274. VBIPecAtr54885_1037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950851 Genomic DNA. Translation: CAG73940.1 .
RefSeqi YP_049136.1. NC_004547.2.

3D structure databases

ProteinModelPortali Q6D8E5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 218491.ECA1029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG73940 ; CAG73940 ; ECA1029 .
GeneIDi 2881763.
KEGGi eca:ECA1029.
PATRICi 20477274. VBIPecAtr54885_1037.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PATR218491:GJNB-1059-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.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCRI 1043 / ATCC BAA-672.

Entry informationi

Entry nameiGLND_PECAS
AccessioniPrimary (citable) accession number: Q6D8E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: August 16, 2004
Last modified: June 11, 2014
This is version 70 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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