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Q6LN22

- GLND_PHOPR

UniProt

Q6LN22 - GLND_PHOPR

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Photobacterium profundum (Photobacterium sp. (strain SS9))
Status
Reviewed - Annotation score: 3 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.UniRule annotation

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 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

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
Ordered Locus Names:PBPRA2970
OrganismiPhotobacterium profundum (Photobacterium sp. (strain SS9))
Taxonomic identifieri74109 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium
ProteomesiUP000000593: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 874874Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192750Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi298386.PBPRA2970.

Structurei

3D structure databases

ProteinModelPortaliQ6LN22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini455 – 588134HDUniRule annotationAdd
BLAST
Domaini696 – 77984ACT 1UniRule annotationAdd
BLAST
Domaini802 – 87473ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 336336UridylyltransferaseAdd
BLAST
Regioni337 – 695359Uridylyl-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

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.

Q6LN22-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIDTSTITNP QTLPVEAITQ ENLRNTLEQF AEQQKQQFIQ HRPVTDLVLS
60 70 80 90 100
RSTFIDKLLI RLWEHYEVNQ YPDIALVAVG GYGRGELHPL SDVDILILSA
110 120 130 140 150
QPLSDETGRI VSKFLTFLWD LRLEVGHSVR TIDDCIEIGN DDLTVATNLT
160 170 180 190 200
EARILCGSED VFQCLQERIN AGNFWPSEDF YRAKLEEQKT RHARYHDTTY
210 220 230 240 250
NLEPDIKSSP GGLRDIHTLS WVARRHFGAT SLLEMSRFGF LTDAEYRELV
260 270 280 290 300
ECQDSLWRIR FALHIELRRY DNRLTFSHQP SVAENLGYTG EGNRGVEMMM
310 320 330 340 350
KEFYRTLRRV LELNKMLLQL FDQAILDNGK TVETIQLSDD FQIRGHLIEA
360 370 380 390 400
TKPALFQARP ETILDMFLHI AQNGDIEGIA APTLRQLRTA RQRLNVFLVD
410 420 430 440 450
IPEAREKFME LVRQPNTLQK AFRLMHRHGV LSAYLPQWSQ IVGQMQFDLF
460 470 480 490 500
HVYTVDEHSV RLIKNLNKFN DPENRERHPI CCEVYPRIIK KELLTIAAIF
510 520 530 540 550
HDIAKGRGGD HSELGAIEAR KFCIQHGLSR PETNLIAWLV QKHLLMSVTA
560 570 580 590 600
QRRDIYDPEV VAEFAKEVRD EERLDYLICL TVADICATNQ ELWNSWKRTL
610 620 630 640 650
LAELYYSTQK ALRRGLENTP DVRDRIRHNQ QLSSAILRGK GFAPREIEVL
660 670 680 690 700
WKRFKADYFL RHTHKQLAWH AEALLTHDHD KPLILLSKKA TRGGTEVFVY
710 720 730 740 750
NKDKAKLFAI VVSELDKKNL SVHDAQIMNS KDGYTLDTFM VLDPSGKTIP
760 770 780 790 800
ENRHNTIRRA LVNALTKMKS ERKNKRAPRK LMHFNVKTQV DFLPTKTGKK
810 820 830 840 850
TTMELIALDT PGLLARIGAV FAKQKVSLQA AKITTIGERA EDFFILVNEH
860 870
GSPLTEEHQQ ALKEALIIKL TPQD
Length:874
Mass (Da):100,797
Last modified:July 5, 2004 - v1
Checksum:iBD18CA770614C067
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR378672 Genomic DNA. Translation: CAG21304.1.
RefSeqiYP_131106.1. NC_006370.1.

Genome annotation databases

EnsemblBacteriaiCAG21304; CAG21304; PBPRA2970.
GeneIDi3123062.
KEGGippr:PBPRA2970.
PATRICi22936978. VBIPhoPro109272_3134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR378672 Genomic DNA. Translation: CAG21304.1 .
RefSeqi YP_131106.1. NC_006370.1.

3D structure databases

ProteinModelPortali Q6LN22.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 298386.PBPRA2970.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG21304 ; CAG21304 ; PBPRA2970 .
GeneIDi 3123062.
KEGGi ppr:PBPRA2970.
PATRICi 22936978. VBIPhoPro109272_3134.

Phylogenomic databases

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

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SS9.

Entry informationi

Entry nameiGLND_PHOPR
AccessioniPrimary (citable) accession number: Q6LN22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 73 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3