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C6DAI1

- GLND_PECCP

UniProt

C6DAI1 - GLND_PECCP

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, PC1_0939
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
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

BioCyciPCAR561230:GKCK-969-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:PC1_0939
OrganismiPectobacterium carotovorum subsp. carotovorum (strain PC1)
Taxonomic identifieri561230 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
ProteomesiUP000002736: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 904904Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000204799Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi561230.PC1_0939.

Structurei

3D structure databases

ProteinModelPortaliC6DAI1.

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.

C6DAI1-1 [UniParc]FASTAAdd to Basket

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MTDNRFSPDS TPPDASSPDS PVDTIASTQL PASPLTYADD MLNCQTLKQQ    50
LELFQLWLGS EFRSGVSAEK LIDARTLFID RLLQRLWYFY GFENIAQTSL 100
VAVGGYGRGE LHPLSDIDVL VLSQTALSEE HSQRVGQFIT LLWDLKLEVG 150
HSVRTLEECL QEGRADISVA TNLIESRMIC GDVALFLTLQ KHVFSDEFWP 200
SSAFFPAKIA 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 LFMNILRHPH AVSRALLPMH 450
RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD EHTIRVLLKL ESFADEETRP 500
QHPLCVELYP RLPQPELLLL AALFHDIAKG RGGDHSELGA QDVLEFAALH 550
GLNSREAQLV SWLVRCHLLM SVTAQRRDIQ DPTVIQQFAT EVQSETRLRY 600
LVSLTVADIC ATNETLWNSW KQSLLRELYF ATEKQLRRGM QNTPDLRERV 650
RHHRLQALAL LRMDNIDEEA LHHIWSRCRA DYFLRHSPNQ LAWHARHLLE 700
HDVNKPLVLI SHQASRGGTE IFIWSPDRPY LFAAVAGELD RRNLSVHDAQ 750
IFTSRDGMAM DTFIVLEPDG SPLAQDRHEM IRHALEQALT QRHYQHPRVR 800
RPSPKLRHFS VPTEVNFLPT HTDRRSYMEL SALDQPGLLA RIGEIFADLN 850
LSLHGARIST IGERVEDLFI LADSDRRALK PELRLKLQER LTEALNPNDK 900
VPLS 904
Length:904
Mass (Da):104,374
Last modified:September 1, 2009 - v1
Checksum:i8B64081DE776F27A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001657 Genomic DNA. Translation: ACT11989.1.
RefSeqiWP_012773628.1. NC_012917.1.
YP_003016525.1. NC_012917.1.

Genome annotation databases

EnsemblBacteriaiACT11989; ACT11989; PC1_0939.
GeneIDi8131868.
KEGGipct:PC1_0939.
PATRICi20486468. VBIPecCar70489_0935.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001657 Genomic DNA. Translation: ACT11989.1 .
RefSeqi WP_012773628.1. NC_012917.1.
YP_003016525.1. NC_012917.1.

3D structure databases

ProteinModelPortali C6DAI1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 561230.PC1_0939.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACT11989 ; ACT11989 ; PC1_0939 .
GeneIDi 8131868.
KEGGi pct:PC1_0939.
PATRICi 20486468. VBIPecCar70489_0935.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PCAR561230:GKCK-969-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. "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
    , Balakrishnan V., Glasner J., Perna N.T.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PC1.

Entry informationi

Entry nameiGLND_PECCP
AccessioniPrimary (citable) accession number: C6DAI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: September 3, 2014
This is version 41 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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