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A3M4Q8

- GLND_ACIBT

UniProt

A3M4Q8 - GLND_ACIBT

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, A1S_1474
Organism
Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
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 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

BioCyciABAU400667:GI0Q-1462-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:A1S_1474
OrganismiAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
Taxonomic identifieri400667 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
ProteomesiUP000006737: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000114748Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi400667.A1S_1474.

Structurei

3D structure databases

ProteinModelPortaliA3M4Q8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini492 – 58695HDAdd
BLAST
Domaini700 – 78283ACT 1Add
BLAST
Domaini809 – 88779ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 337337UridylyltransferaseUniRule annotationAdd
BLAST
Regioni339 – 699361Uridylyl-removingUniRule annotationAdd
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.
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.

A3M4Q8-1 [UniParc]FASTAAdd to Basket

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MINTSPLLNY VSSHHDIKAI NQWRTDVEKQ LQDSYENGQS IREIIKARSD    50
LVDEALVFLW KHAELDQSKL GLFAVGGYGR REMLPYSDVD IMILSEDEIS 100
EENEKRISTF ISSLWDVGNF KPGISVRTIQ SCVEQAATDL TVATTLIEAR 150
LITGNTQLAK WPRRIVSQTW TDKTFYDAKM AEQAKRYHQH NNTESNLEPD 200
IKNAPGGIRD INQIGWIAKR HFRVNRIYDL VHLGFISEFE LAVLEEAESF 250
LWEIRHHLHR LAKRDENRLL FDHQREIAAK FGYVRQEGQP VNYGVEQFMK 300
RYYRTAQQVS TLNEMLLAYF SESVITPRLP NYERKIEVVN DHFKIVDNKL 350
AVQHHKIFAE HPSAILELFY ILANRPDIEG IRARTLRLLI LAAKRINQSY 400
RDNPEHQALF MSIIRSPYRL YDTLVAMKRY GVLGNYIPAF GQIMGLMQYD 450
LFHIYTVDAH TLLLLRNLNR FREPEFAKEF PVVSSVFQRL ARQDIVFIAA 500
LFHDIAKGRG GDHSELGAED AIEFGRAHGF TERECKLIAW LIQNHLLMSL 550
TAQKKDISDP DVVKDFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 600
SLMRQLYTHA RDVIRTGLGR PVDYQMLIED TKFAASELLV NNFALADVEK 650
VWQELGDEYF IKESADEIAW HTQAILKHGD NPEPLVLLRA HRKAAQDAVQ 700
IFIYTRDQPN LFATTVAVLD RMNLDVQDAK IITASTAFSL DTYVVLDRFG 750
TLLTDPEREE TVKNALVKAL SQPDQYPGLM QRRIPRQLRH FDIENTVDVT 800
LNEALQQNMV EISTLDHPGL LARVGGLFMM QGLDIHSARI ATLGERAEDI 850
FFVTKKDGKP LNHEEVKLFS EKLKAALDEA SNQICQH 887
Length:887
Mass (Da):102,126
Last modified:September 2, 2008 - v2
Checksum:i5D8D5FB823A833F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000521 Genomic DNA. Translation: ABO11902.2.

Genome annotation databases

EnsemblBacteriaiABO11902; ABO11902; A1S_1474.
PATRICi20719190. VBIAciBau103176_1504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000521 Genomic DNA. Translation: ABO11902.2 .

3D structure databases

ProteinModelPortali A3M4Q8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 400667.A1S_1474.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO11902 ; ABO11902 ; A1S_1474 .
PATRICi 20719190. VBIAciBau103176_1504.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci ABAU400667:GI0Q-1462-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. "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
    Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
    Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17978 / NCDC KC 755.

Entry informationi

Entry nameiGLND_ACIBT
AccessioniPrimary (citable) accession number: A3M4Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: June 11, 2014
This is version 58 of the entry and version 2 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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