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Q9AC53

- GLND_CAUCR

UniProt

Q9AC53 - GLND_CAUCR

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Caulobacter crescentus (strain ATCC 19089 / CB15)
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:CC_0013
OrganismiCaulobacter crescentus (strain ATCC 19089 / CB15)
Taxonomic identifieri190650 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001816: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 940940Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192727Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9AC53.
SMRiQ9AC53. Positions 397-585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini497 – 627131HDUniRule annotationAdd
BLAST
Domaini737 – 82185ACT 1UniRule annotationAdd
BLAST
Domaini848 – 92982ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 379379UridylyltransferaseAdd
BLAST
Regioni380 – 736357Uridylyl-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.
HOGENOMiHOG000261779.
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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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.

Q9AC53-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRRLRPTRL EHVVDGHALR ARLSAAALDS IGNEAEQRAR AIDILKQALF
60 70 80 90 100
RGRMIAKERL ENGASGVETS RLLSGVTDEV ITALYDFTTV HVFRARNPTE
110 120 130 140 150
GERLCLLAVG GYGRGTLAPF SDIDLLFLRP YKQTPHAESV IEYMLYALWD
160 170 180 190 200
LGFKVGHASR TIEECVRLSK EDFTIRTSIL EARRLTGDER LAEDLKKRFR
210 220 230 240 250
DEVMKATGAQ FVAAKLKERD DRQARAGASR YMVEPNVKEG KGGLRDLHTL
260 270 280 290 300
MWIAEYLHPV DRPEDVFKME VFSIRETKAF IRAFDFLHAV RAHLHFTTGR
310 320 330 340 350
PEERLTFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLIAK EVGTLTRAFS
360 370 380 390 400
AKLEAEHFKN EPKGISRFLP GARPKRKALD VEGFYEDGGR LNIEGQEIFE
410 420 430 440 450
ADPVNLIRLF KIADERDLDL HPDAFTAVTR ALPLITSRVR RDPDACRAFL
460 470 480 490 500
DLLARGKRSY RTLTLMNDAG VLGRFIPEFG RVVAQMQFNM YHSYTVDEHT
510 520 530 540 550
LRAVGVIGDI AAGRLVDDHP LAVSIMPLIE DREALFLAML LHDTGKGGVG
560 570 580 590 600
GQEKAGARSA RSACERLGVE RSKVELVAWL VENHLVMSDF AQKRDVSDPG
610 620 630 640 650
TVAAFARIVE NPERLRLLLV ITVADIRAVG PGVWNGWKGQ LLRELYNATE
660 670 680 690 700
AVFRGGRGSD AAANVQRHQE STAEAARAAL LETDPAAKGW VAAMENAYFS
710 720 730 740 750
AFSQDDLFHH AELARRAAIQ GGAAAEGQVR PGSNAAEVVI AAKDRRGLFA
760 770 780 790 800
DLALAISSLG GNVVGARVFT SRQGQALDVF YVQDVTGAPF GCENPRALRR
810 820 830 840 850
LADALEAAGK GDALAVEPRR GSEQTRAAAF AIAPSVTIDN DASNDATVVE
860 870 880 890 900
ASGRDRPGLL HALAKTLADS ALSIQSAHID GYGERAVDAF YVQTTEGGKV
910 920 930 940
TDTRKLNALK ADLLAALEQN EASAPAARPG LRRARASVAR
Length:940
Mass (Da):103,396
Last modified:June 1, 2001 - v1
Checksum:i2F1985420353F8ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005673 Genomic DNA. Translation: AAK22001.1.
PIRiE87250.
RefSeqiNP_418833.1. NC_002696.2.
WP_010917903.1. NC_002696.2.

Genome annotation databases

EnsemblBacteriaiAAK22001; AAK22001; CC_0013.
GeneIDi940508.
KEGGiccr:CC_0013.
PATRICi21296948. VBICauCre124313_0014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005673 Genomic DNA. Translation: AAK22001.1 .
PIRi E87250.
RefSeqi NP_418833.1. NC_002696.2.
WP_010917903.1. NC_002696.2.

3D structure databases

ProteinModelPortali Q9AC53.
SMRi Q9AC53. Positions 397-585.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK22001 ; AAK22001 ; CC_0013 .
GeneIDi 940508.
KEGGi ccr:CC_0013.
PATRICi 21296948. VBICauCre124313_0014.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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: ATCC 19089 / CB15.

Entry informationi

Entry nameiGLND_CAUCR
AccessioniPrimary (citable) accession number: Q9AC53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 87 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