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B2HYT7

- GLND_ACIBC

UniProt

B2HYT7 - GLND_ACIBC

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Acinetobacter baumannii (strain ACICU)
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

BioCyciABAU405416:GI27-1549-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:ACICU_01512
OrganismiAcinetobacter baumannii (strain ACICU)
Taxonomic identifieri405416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
ProteomesiUP000008839: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114746Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi405416.ACICU_01512.

Structurei

3D structure databases

ProteinModelPortaliB2HYT7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini492 – 58695HDUniRule annotationAdd
BLAST
Domaini700 – 78283ACT 1UniRule annotationAdd
BLAST
Domaini809 – 88779ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 337337UridylyltransferaseAdd
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.

B2HYT7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MINTSPLLNY VSSHHDIKAI NQWRTDVEKQ LQDSYENGQS IREIIKARSD
60 70 80 90 100
LVDEALVFLW KHAELDQSKL GLFAVGGYGR REMLPYSDVD IMILSEDEIS
110 120 130 140 150
EENEKRISTF ISSLWDVGNF KPGISVRTIQ SCVEQAATDL TVATTLIEAR
160 170 180 190 200
LITGNTQLAK WPRRIVSQTW TDKTFYDAKM AEQAKRYHQH NNTESNLEPD
210 220 230 240 250
IKNAPGGIRD INQIGWIAKR HFRVNRIYDL VHLGFISEFE LAVLEEAESF
260 270 280 290 300
LWEIRHHLHR LAKRDENRLL FDHQREIAAK FGYVRQEGQP VNYGVEQFMK
310 320 330 340 350
RYYRTAQQVS TLNEMLLAYF SESVITPRLP NYERKIEVVN DHFKIVDNKL
360 370 380 390 400
AVQHHKIFAE HPSAILELFY ILANRPDIEG IRARTLRLLI LAAKRINQSY
410 420 430 440 450
RDNPEHQALF MSIIRSPYRL YDTLVAMKRY GVLGNYIPAF AQIMGLMQYD
460 470 480 490 500
LFHIYTVDAH TLLLLRNLNR FREPEFAKEF PVVSSVFQRL ARQDIVFIAA
510 520 530 540 550
LFHDIAKGRG GDHSELGAED AIEFGRAHGF TERECKLIAW LIQNHLLMSL
560 570 580 590 600
TAQKKDISDP DVVKDFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA
610 620 630 640 650
SLMRQLYTHA RDVIRTGLGR PVDYQMLIED TKFAASELLV NNFALADVEK
660 670 680 690 700
VWQELGDEYF IKESADEIAW HTQAILKHGD NPEPLVLLRA HRKAAQDAVQ
710 720 730 740 750
IFIYTRDQPN LFATTVAVLD RMNLDVQDAK IITASTAFSL DTYVVLDRFG
760 770 780 790 800
TLLTDPEREE TVKNALVKAL SQPDQYPGLM QRRIPRQLRH FDIENTVDVT
810 820 830 840 850
LNEALQQNMV EISTLDHPGL LARVGGLFMM QGLDIHSARI ATLGERAEDI
860 870 880
FFVTKKDGKP LNNEEVKLFS EKLKAALDEA SNQICQH
Length:887
Mass (Da):102,117
Last modified:June 10, 2008 - v1
Checksum:iB56AC50301F12C64
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000863 Genomic DNA. Translation: ACC56824.1.
RefSeqiWP_000611175.1. NC_010611.1.
YP_001846171.1. NC_010611.1.

Genome annotation databases

EnsemblBacteriaiACC56824; ACC56824; ACICU_01512.
GeneIDi6235261.
KEGGiabc:ACICU_01512.
PATRICi20711789. VBIAciBau103538_1586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000863 Genomic DNA. Translation: ACC56824.1 .
RefSeqi WP_000611175.1. NC_010611.1.
YP_001846171.1. NC_010611.1.

3D structure databases

ProteinModelPortali B2HYT7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405416.ACICU_01512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACC56824 ; ACC56824 ; ACICU_01512 .
GeneIDi 6235261.
KEGGi abc:ACICU_01512.
PATRICi 20711789. VBIAciBau103538_1586.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ABAU405416:GI27-1549-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. "Whole-genome pyrosequencing of an epidemic multidrug-resistant Acinetobacter baumannii strain belonging to the European clone II group."
    Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.
    Antimicrob. Agents Chemother. 52:2616-2625(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ACICU.

Entry informationi

Entry nameiGLND_ACIBC
AccessioniPrimary (citable) accession number: B2HYT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: October 29, 2014
This is version 46 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