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A6U5G1

- GLND_SINMW

UniProt

A6U5G1 - GLND_SINMW

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, Smed_0031
Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
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

BioCyciSMED366394:GJAL-31-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:Smed_0031
OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
Taxonomic identifieri366394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001108: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000022354Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi366394.Smed_0031.

Structurei

3D structure databases

ProteinModelPortaliA6U5G1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini494 – 608115HDAdd
BLAST
Domaini734 – 81582ACT 1Add
BLAST
Domaini845 – 92682ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 377377UridylyltransferaseUniRule annotationAdd
BLAST
Regioni378 – 733356Uridylyl-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.
HOGENOMiHOG000261779.
KOiK00990.
OMAiLYCLWDM.
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.

A6U5G1-1 [UniParc]FASTAAdd to Basket

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MARHETSFPE ILDVAALRAR CDFIASAHAE QREPMRRALL AAFKEANIAG    50
RAKARELLAA DGAGIKCAER ISWLQDQLIT LLHDFVLNQV FDAAKAPETS 100
RIAVTAVGGY GRGTLAPGSD IDLLFLLPAK KAVWAEPAIE FMLYILWDLG 150
FKVGHATRTI EDCIRLSRAD MTIRTAILEC RYVCGSVALA SELETRFDHE 200
IVRNTGPEFI AAKLAERDER HRKAGDTRYL VEPNVKEGKG GLRDLHTLFW 250
ISKYFYRVKD SADLVKLGVL SRQEYKLFQK AEDFLWAVRC HMHFLTGKAE 300
ERLSFDIQRE IAEALGYHDH PGLSAVERFM KHYFLVAKDV GDLTRIFCSA 350
LEDQQAKDAP GISGVISRFR NRVRKIPGTL DFVDDGGRIA LASPDVFKRD 400
PVNLLRMFHI ADINGLEFHP AALKQVTRSL SLITPHLREN EEANRLFLSI 450
LTSRRNPELI LRRMNEAAVL GRFIPEFGKI VSMMQFNMYH HYTVDEHLLR 500
AVDVLSRIER GLEEEAHPLT AMLMPAIEDR EALYVAVLLH DIAKGRPEDH 550
SVAGAKVARK LCPRFRLSPK QTETVVWLVE EHLTMSMVAQ TRDLNDRKTI 600
VDFAERVQSL ERLKMLLILT VCDIRAVGPG VWNGWKGQLL RTLYYETELL 650
LSGGFSELSR KERAKHAADM LEEALADWPK EERQTYVRLH YQPYLLTVAL 700
DEQVRHAAFI READAAGRTL ATMVRTHDFH AITEITVLSP DHPRLLTVIA 750
GACAAAGANI VGAQIHTTSD GRALDTILVN REFSVAEDET RRAASIGKLI 800
EDVLSGRKKL PDVIASRTRS KKRSRAFTVT PEVTISNALS NKFTVIEVEG 850
LDRTGLLSEV TAVLSDLSLD IASAHITTFG EKVIDTFYVT DLVGSKITSE 900
NRQMNIAARL KAVLAGEVDE ARERMPSGII APTPVPRASH GSKATKAET 949
Length:949
Mass (Da):106,228
Last modified:August 21, 2007 - v1
Checksum:iE18E0283457CC20C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000738 Genomic DNA. Translation: ABR58891.1.
RefSeqiYP_001325726.1. NC_009636.1.

Genome annotation databases

EnsemblBacteriaiABR58891; ABR58891; Smed_0031.
GeneIDi5320858.
KEGGismd:Smed_0031.
PATRICi23618827. VBISinMed134228_3085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000738 Genomic DNA. Translation: ABR58891.1 .
RefSeqi YP_001325726.1. NC_009636.1.

3D structure databases

ProteinModelPortali A6U5G1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 366394.Smed_0031.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR58891 ; ABR58891 ; Smed_0031 .
GeneIDi 5320858.
KEGGi smd:Smed_0031.
PATRICi 23618827. VBISinMed134228_3085.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
KOi K00990.
OMAi LYCLWDM.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci SMED366394:GJAL-31-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 Sinorhizobium medicae WSM419 chromosome."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WSM419.

Entry informationi

Entry nameiGLND_SINMW
AccessioniPrimary (citable) accession number: A6U5G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: June 11, 2014
This is version 55 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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