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Q8PMJ8

- GLND_XANAC

UniProt

Q8PMJ8 - GLND_XANAC

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, XAC1429
Organism
Xanthomonas axonopodis pv. citri (strain 306)
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

BioCyciXAXO190486:GH55-1429-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:XAC1429
OrganismiXanthomonas axonopodis pv. citri (strain 306)
Taxonomic identifieri190486 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000000576: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192776Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi190486.XAC1429.

Structurei

3D structure databases

ProteinModelPortaliQ8PMJ8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 570120HD
Add
BLAST
Domaini692 – 77483ACT 1
Add
BLAST
Domaini798 – 86972ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 332332UridylyltransferaseUniRule annotation
Add
BLAST
Regioni333 – 691359Uridylyl-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. 1 hit.
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.

Q8PMJ8-1 [UniParc]FASTAAdd to Basket

« Hide

MTDTPAERPD PGVAGDADWA AQARPLLVHV DMRLCKRFDQ GEPIERLVAL    50
RARAVDQLMR NAWMRCIPAD SGLSLHAVGG YGRGELFPRS DVDVLVLGDT 100
AAQQQHEQAL ARLFALLWDV GLPISHAVRS PAQCTAAAAD QTVLTALIES 150
RALVADAQAR AALATAIAPP QVWPPRDFFQ AKREELLARH QRFGDTADNL 200
EPDIKDGPGG LRDLQTLGWM ALRAFGVKDL EALVGLGHVG FDEAAALRRE 250
REELARLRFG LHIVANRPEE RLRFDYQKTL AERLGFADDP ESLGVEKMMQ 300
RFYRSAALIR RISDRLLQRF EEQFDGEATP EPLGGGFSLR RGYLAADTES 350
WPDGDVLQVF ALFAQWAAHR EVRGLHSLTA RALAEVLRDL PAYEVADATA 400
RERFMALLRG PRAVETLNRM ARLGVLGQWI PAFASVSGRM QFDLFHVYTV 450
DQHTLMVLRN IALFAAGRAD EHFSIAHEVW PRLRKPELLL LAGLFHDIAK 500
GRGGDHSELG AVDARAFCLA HRLSEGDTEL VTWLVEQHLR MSVTAQKQDI 550
SDPEVIHRFA TLVGTRERLD YLYLLTCADI AGTSPKLWNA WKDRLLADLY 600
FAARRALREG LEHPPPREER LREARESART LMQAQGHDDV TIDRQFAGMP 650
DENFLRFRPE QLAWQAASLI EVEIGQTLVK ARRAVPDNDA LEVFVYSPDR 700
DGLFAAIVAT LDRKGYGIHR ARVLDAPHDA IFDVFEVLPQ ETYADGDPQR 750
LAATLRQVLA GDLQKVRPAR RAVPRQLRHF RFAPRVEFSE SAGGRRTRIS 800
LVAPDRPGLL ADVAHVLRMQ HLRVHDARIA TFGERAEDQF QITDEHDRPL 850
SESARQALRD ALCACLDPV 869
Length:869
Mass (Da):97,370
Last modified:October 10, 2002 - v1
Checksum:i407F906188598799
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008923 Genomic DNA. Translation: AAM36300.1.
RefSeqiNP_641764.1. NC_003919.1.
WP_011050907.1. NC_003919.1.

Genome annotation databases

EnsemblBacteriaiAAM36300; AAM36300; XAC1429.
GeneIDi1155500.
KEGGixac:XAC1429.
PATRICi24054857. VBIXanAxo33670_1509.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008923 Genomic DNA. Translation: AAM36300.1 .
RefSeqi NP_641764.1. NC_003919.1.
WP_011050907.1. NC_003919.1.

3D structure databases

ProteinModelPortali Q8PMJ8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 190486.XAC1429.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM36300 ; AAM36300 ; XAC1429 .
GeneIDi 1155500.
KEGGi xac:XAC1429.
PATRICi 24054857. VBIXanAxo33670_1509.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci XAXO190486:GH55-1429-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. 1 hit.
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. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 306.

Entry informationi

Entry nameiGLND_XANAC
AccessioniPrimary (citable) accession number: Q8PMJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: September 3, 2014
This is version 84 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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