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Q6FAM5

- GLND_ACIAD

UniProt

Q6FAM5 - GLND_ACIAD

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
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

Magnesium.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

Enzyme and pathway databases

BioCyciASP62977:GJVV-1960-MONOMER.

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:ACIAD2079
OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Taxonomic identifieri62977 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
ProteomesiUP000000430: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 888888Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192713Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi62977.ACIAD2079.

Structurei

3D structure databases

ProteinModelPortaliQ6FAM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini491 – 58696HDUniRule annotationAdd
BLAST
Domaini700 – 78182ACT 1UniRule annotationAdd
BLAST
Domaini809 – 88779ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 338338UridylyltransferaseAdd
BLAST
Regioni339 – 699361Uridylyl-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.

Q6FAM5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIITSPLLDY VTSHQDIKAI NQWRADVEQQ LQEFYENGYS IRDIVLARSN
60 70 80 90 100
LIDEALTFLW KHAGLDQSDL GLFAVGGYGR REMLPYSDVD IMILSENDIS
110 120 130 140 150
PEHEKQISGF ISSLWDVGNF KPGTSVRSIQ NCVEQATNDL TVATTLIESR
160 170 180 190 200
LITGNPDLAK WPRRIVSQTW TDKTFFDAKM EEQAKRHAQH NNTESNLEPD
210 220 230 240 250
IKNAPGGIRD MNQIGWIAKR HFRVNRIYDL VHLGFITEYE LKVLEEAESF
260 270 280 290 300
LWEIRHHLHL LSKRDENRLL FDHQREIAAK FGYTRAEGQP VNFAVEQFMK
310 320 330 340 350
RYYRTAQQVS TLNEMLLAYF NESVITPRLP NYERKIEEIN ENFKLVDGKL
360 370 380 390 400
AVQHHKVFSE NPSAILELFY LLANHPEIEG IRARTLRLLI MAAKRIDQEF
410 420 430 440 450
RDNPAHQALF MAIIRSPYRL YDTLVDMKRY GILGNYIPAF GQIMGLMQYD
460 470 480 490 500
LFHIYTVDAH TLLLIRNLNR FKEPEFAQHF PVVSSVFQRL ARRDIVYLAA
510 520 530 540 550
IFHDIAKGRG GDHSELGAED AIEFCRAHGF TERECKLVAW LIHNHLLMSL
560 570 580 590 600
TAQKKDISDP DVIKEFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA
610 620 630 640 650
SLMRQLYTYS RDVIRSGLGR PVDYQMLIED TKFSASETLV NEFSLDAVEK
660 670 680 690 700
VWQELGDEYF LKESADEIAW HTRAILQHGD NPAPIVLLRA HRQSAQDAVQ
710 720 730 740 750
IFIYTQDKPN LFATTVAVLD RMNLDVQDAR IITATKAFSL DTYVVLDRFG
760 770 780 790 800
TLLTDPEREH TVKEALIKAL SQSDKYPGLM QRRIPRQLRH FDIENTVDIT
810 820 830 840 850
LNPVLQQNMV EISTLDQPGL LARVGGLFMM QGLDIHSAKI ATLGERAEDI
860 870 880
FFVTKKDGQP MTTDEAHIFS AQLKLALDEA SNQIVSQH
Length:888
Mass (Da):102,208
Last modified:July 19, 2004 - v1
Checksum:i1F244D77538E36FC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR543861 Genomic DNA. Translation: CAG68888.1.
RefSeqiYP_046710.1. NC_005966.1.

Genome annotation databases

EnsemblBacteriaiCAG68888; CAG68888; ACIAD2079.
GeneIDi2881141.
KEGGiaci:ACIAD2079.
PATRICi20741848. VBIAciSp98416_1868.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR543861 Genomic DNA. Translation: CAG68888.1 .
RefSeqi YP_046710.1. NC_005966.1.

3D structure databases

ProteinModelPortali Q6FAM5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 62977.ACIAD2079.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG68888 ; CAG68888 ; ACIAD2079 .
GeneIDi 2881141.
KEGGi aci:ACIAD2079.
PATRICi 20741848. VBIAciSp98416_1868.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ASP62977:GJVV-1960-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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
    Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
    Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33305 / BD413 / ADP1.

Entry informationi

Entry nameiGLND_ACIAD
AccessioniPrimary (citable) accession number: Q6FAM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 19, 2004
Last modified: October 29, 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