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P36223

- GLND_AZOVI

UniProt

P36223 - GLND_AZOVI

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Modifies, by uridylylation and deuridylylation, the PII regulatory protein GlnK, 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 protein 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 protein, and plays an important role in the regulation of nitrogen fixation and metabolism.2 Publications

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen fixation Source: UniProtKB-KW
  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

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
Synonyms:nfrX
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are not viable unless a second mutation occurs, either spontaneously or by design, resulting in the inability of glutamine synthetase (GS) to be adenylylated.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 899899Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192717Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP36223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini486 – 590105HDUniRule annotationAdd
BLAST
Domaini706 – 78984ACT 1UniRule annotationAdd
BLAST
Domaini816 – 89984ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342UridylyltransferaseAdd
BLAST
Regioni343 – 705363Uridylyl-removingAdd
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.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.UniRule annotation
Contains 2 ACT domains.UniRule annotation
Contains 1 HD domain.UniRule annotation

Keywords - Domaini

Repeat

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.

P36223-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQVDPDLFD PGQFQAELAL KSSPIPAYKK ALRCAREVLD ARFQEGRDIR
60 70 80 90 100
RLIEDRAWFV DQILALAWNR FDWSEDADIA LIAVGGYGRG ELHPYSDIDL
110 120 130 140 150
LILMDGADHE VFREPIEGFL TLLWDIGLEV GQSVRSLAEC AEEAQADLTV
160 170 180 190 200
ITNLMESRTI AGPEHLRQRM QEVTSAQRMW PSRAFFLAKR DEQKTRHARY
210 220 230 240 250
NDTEYNLEPN VKGSPGGLRD IQTLLWIARR QFGTINLHAM VGQGFLLESE
260 270 280 290 300
YTLLASSQEF LWKVRYALHM LAGRAEDRLL FDLQRQIAGL LGYEDSDAKL
310 320 330 340 350
AVERFMQKYY RVVLGIAELT ELVFQHFEEV ILPGDAAGRV EPLNERFQVR
360 370 380 390 400
DGYLEVTHAG VFQETPSALL EIFVLLARRP EIRGVRADTI RLLRDHRYLI
410 420 430 440 450
DDAFRRDPHN TGLFIELFKS RQGIHRNLRR MNRYGILGRY LPEFGHIVGQ
460 470 480 490 500
MQHDLFHIYT VDAHTLNLIK NLRKLFWPEL AEKYPLASKL IEKLPKPELI
510 520 530 540 550
YLAGLYHDIG KGRGGDHSEL GAADALAFCQ RHDLPAMDTQ LIVWLVRNHL
560 570 580 590 600
LMSTTAQRKD LSDPQVIFDF AQKVRDQTYL DYLYVLTVAD INATNPTLWN
610 620 630 640 650
SWRASLLRQL YTETKHALRR GLEQPVGREE QIRQTQKAAL DILVRSGTDP
660 670 680 690 700
DDAEHLWTQL GDDYFLRHTS SDIAWHTEAI LQHPSSGGPL VLIKETTQRE
710 720 730 740 750
FEGATQIFIY APDQHDFFAV TVAAMDQLNL SIHDARVITS TSQFTLDTYI
760 770 780 790 800
VLDADGGSIG NNPARIQEIR QGLVEALRNP ADYPTIIQRR VPRQLKHFAF
810 820 830 840 850
APQVTIQNDA LRPVTILEII APDRPGLLAR IGKIFLDFDL SLQNAKIATL
860 870 880 890
GERVEDVFFV TDAHNQPLSD PELCARLQLA IAEQLADGDS YIQPSRISI
Length:899
Mass (Da):102,580
Last modified:June 1, 1994 - v1
Checksum:i96AF63BC5EDE3C9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59610 Genomic DNA. Translation: CAA42173.1.
PIRiS24223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59610 Genomic DNA. Translation: CAA42173.1 .
PIRi S24223.

3D structure databases

ProteinModelPortali P36223.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "The product of the nitrogen fixation regulatory gene nfrX of Azotobacter vinelandii is functionally and structurally homologous to the uridylyltransferase encoded by glnD in enteric bacteria."
    Contreras A., Drummond M., Bali A., Blanco G., Garcia E., Bush G., Kennedy C., Merrick M.
    J. Bacteriol. 173:7741-7749(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COMPLEMENTATION OF E.COLI GLND MUTANT, ROLE IN NITROGEN FIXATION.
    Strain: OP / UW136.
  2. "Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation."
    Colnaghi R., Rudnick P., He L., Green A., Yan D., Larson E., Kennedy C.
    Microbiology 147:1267-1276(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PII URIDYLYLTRANSFERASE, DISRUPTION PHENOTYPE.
    Strain: OP / UW136.

Entry informationi

Entry nameiGLND_AZOVI
AccessioniPrimary (citable) accession number: P36223
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 75 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3