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A5U6S3

- GLND_MYCTA

UniProt

A5U6S3 - GLND_MYCTA

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, MRA_2943
Organism
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
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

BioCyciMTUB419947:GJ8N-3043-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:MRA_2943
OrganismiMycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Taxonomic identifieri419947 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001988: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 808808Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000022346Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi419947.MRA_2943.

Structurei

3D structure databases

ProteinModelPortaliA5U6S3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini431 – 536106HDAdd
BLAST
Domaini610 – 68677ACT 1Add
BLAST
Domaini730 – 80576ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 315315UridylyltransferaseUniRule annotationAdd
BLAST
Regioni316 – 609294Uridylyl-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.
HOGENOMiHOG000021840.
KOiK00990.
OMAiRRPIDEG.
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. 1 hit.
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.

A5U6S3-1 [UniParc]FASTAAdd to Basket

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MEAESPCAAS DLAVARRELL SGNHRELDPV GLRQTWLDLH ESWLIDKADE    50
IGIADASGFA IVGVGGLGRR ELLPYSDLDV LLLHDGKPAD ILRPVADRLW 100
YPLWDANIRL DHSVRTVSEA LTIANSDLMA ALGMLEARHI AGDQQLSFAL 150
IDGVRRQWRN GIRSRMGELV EMTYARWRRC GRIAQRAEPD LKLGRGGLRD 200
VQLLDALALA QLIDRHGIGH TDLPAGSLDG AYRTLLDVRT ELHRVSGRGR 250
DHLLAQFADE ISAALGFGDR FDLARTLSSA GRTIGYHAEA GLRTAANALP 300
RRGISALVRR PKRRPLDEGV VEYAGEIVLA RDAEPEHDPG LVLRVAAASA 350
DTGLPIGAAT LSRLAASVPD LPTPWPQEAL DDLLVVLSAG PTTVATIEAL 400
DRTGLWGRLL PEWEPIRDLP PRDVAHKWTV DRHVVETAVH AAPLATRVAR 450
PDLLALGALL HDIGKGRGTD HSVLGAELVI PVCTRLGLSP PDVRTLSKLV 500
RHHLLLPITA TRRDLNDPKT IEAVSEALGG DPQLLEVLHA LSEADSKATG 550
PGVWSDWKAS LVDDLVRRCR MVMAGESLPQ AEPTAPHYLS LAADHGVHVE 600
ISPRDGERID AVIVAPDERG LVSKAAAVLA LNSLRVHSAS VNVHQGVAIT 650
EFVVSPLFGS PPAAELVRQQ FVGALNGDVD VLGMLQKRDS DAASLVSARA 700
GDVQAGVPVT RTAAPPRILW LDTAAPAKLI LEVRAMDRAG LLALLAGALE 750
GAGAGIVWAK VNTFGSTAAD VFCVTVPAEL DARAAVEQHL LEVLGASVDV 800
VVDEPVGD 808
Length:808
Mass (Da):86,438
Last modified:July 10, 2007 - v1
Checksum:i9B1F14D01C29F0B0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000611 Genomic DNA. Translation: ABQ74723.1.
RefSeqiYP_001284285.1. NC_009525.1.

Genome annotation databases

EnsemblBacteriaiABQ74723; ABQ74723; MRA_2943.
GeneIDi5215487.
KEGGimra:MRA_2943.
PATRICi18146209. VBIMycTub106795_3293.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000611 Genomic DNA. Translation: ABQ74723.1 .
RefSeqi YP_001284285.1. NC_009525.1.

3D structure databases

ProteinModelPortali A5U6S3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 419947.MRA_2943.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ74723 ; ABQ74723 ; MRA_2943 .
GeneIDi 5215487.
KEGGi mra:MRA_2943.
PATRICi 18146209. VBIMycTub106795_3293.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000021840.
KOi K00990.
OMAi RRPIDEG.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci MTUB419947:GJ8N-3043-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. 1 hit.
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. "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
    Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25177 / H37Ra.

Entry informationi

Entry nameiGLND_MYCTA
AccessioniPrimary (citable) accession number: A5U6S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 58 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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