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Q83MD4

- GLND_SHIFL

UniProt

Q83MD4 - GLND_SHIFL

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Shigella flexneri
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

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:SF0157, S0160
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192768Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi198214.SF0157.

Structurei

3D structure databases

ProteinModelPortaliQ83MD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 601134HDUniRule annotationAdd
BLAST
Domaini709 – 78981ACT 1UniRule annotationAdd
BLAST
Domaini816 – 89075ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 349349UridylyltransferaseAdd
BLAST
Regioni350 – 708359Uridylyl-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. 2 hits.
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.

Q83MD4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTLPEQYAN TALSTLPGQP QNPCAWPRDE LTVCGIKAHI DTFQRWLGDA
60 70 80 90 100
FDNGISAEQL IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL
110 120 130 140 150
HPLSDIDLLI LSRKKLPDDQ AQKVGELLTL LWDVKLEVGH SVRTLEECML
160 170 180 190 200
EGLSDLTVAT NLIESRLLIG DVALFLELQK HIFSEGFWPS DKFYAAKVEE
210 220 230 240 250
QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG
260 270 280 290 300
FGFLTSAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN
310 320 330 340 350
YSGEGNEPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPL
360 370 380 390 400
DDEFQLRGTL IDLRDETLFM RQPEAILRMF YTMVRNSAIT GIYSTTLRQL
410 420 430 440 450
RHARRHLQQP LCNIPQARKL FLSILRHPGA VRRGLLPMHR HSVLGAYMPQ
460 470 480 490 500
WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFASEETRQR HPLCVDVWPR
510 520 530 540 550
LPSTELIFIA ALFHDIAKGR GGDHSILGAQ DVVHFAELHG LNSRETQLVA
560 570 580 590 600
WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTENRLRYL VCLTVADICA
610 620 630 640 650
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL
660 670 680 690 700
RMDNIDEEAL HQIWSRCRAN YFVRHSPNQL AWHARHLLQH DLSKPLVLLS
710 720 730 740 750
PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD
760 770 780 790 800
TFIVLEPDGS PLSADRHEVI RFGLEQVLTQ SSWQPPQPRR QPAKLRHFTV
810 820 830 840 850
ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI SLHGARITTI
860 870 880 890
GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG
Length:890
Mass (Da):102,403
Last modified:June 1, 2003 - v1
Checksum:i1B382E6170E8440A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN41819.1.
AE014073 Genomic DNA. Translation: AAP15700.1.
RefSeqiNP_706112.1. NC_004337.2.
NP_835895.1. NC_004741.1.
WP_001094600.1. NZ_JMRK01000015.1.

Genome annotation databases

EnsemblBacteriaiAAN41819; AAN41819; SF0157.
AAP15700; AAP15700; S0160.
GeneIDi1024456.
1076593.
KEGGisfl:SF0157.
sfx:S0160.
PATRICi18701268. VBIShiFle31049_0175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN41819.1 .
AE014073 Genomic DNA. Translation: AAP15700.1 .
RefSeqi NP_706112.1. NC_004337.2.
NP_835895.1. NC_004741.1.
WP_001094600.1. NZ_JMRK01000015.1.

3D structure databases

ProteinModelPortali Q83MD4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF0157.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN41819 ; AAN41819 ; SF0157 .
AAP15700 ; AAP15700 ; S0160 .
GeneIDi 1024456.
1076593.
KEGGi sfl:SF0157.
sfx:S0160.
PATRICi 18701268. VBIShiFle31049_0175.

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. 2 hits.
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. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiGLND_SHIFL
AccessioniPrimary (citable) accession number: Q83MD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 82 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