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B8GWX0

- GLND_CAUCN

UniProt

B8GWX0 - GLND_CAUCN

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, CCNA_00013
Organism
Caulobacter crescentus (strain NA1000 / CB15N)
Status
Reviewed - Annotation score: 4 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

BioCyciCAULONA1000:CCNA_00013-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:CCNA_00013
OrganismiCaulobacter crescentus (strain NA1000 / CB15N)
Taxonomic identifieri565050 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001364: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 940940Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000132527Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi190650.CC_0013.

Structurei

3D structure databases

ProteinModelPortaliB8GWX0.
SMRiB8GWX0. Positions 386-632.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini497 – 627131HD
Add
BLAST
Domaini737 – 82185ACT 1
Add
BLAST
Domaini848 – 92982ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 379379UridylyltransferaseUniRule annotation
Add
BLAST
Regioni380 – 736357Uridylyl-removingUniRule annotation
Add
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.
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.

B8GWX0-1 [UniParc]FASTAAdd to Basket

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MPRRLRPTRL EHVVDGHALR ARLSAAALDS IGNEAEQRAR AIDILKQALF    50
RGRMIAKERL ENGASGVETS RLLSGVTDEV ITALYDFTTV HVFRARNPTE 100
GERLCLLAVG GYGRGTLAPF SDIDLLFLRP YKQTPHAESV IEYMLYALWD 150
LGFKVGHASR TIEECVRLSK EDFTIRTSIL EARRLTGDER LAEDLKKRFR 200
DEVMKATGAQ FVAAKLKERD DRQARAGASR YMVEPNVKEG KGGLRDLHTL 250
MWIAEYLHPV DRPEDVFKME VFSIRETKAF IRAFDFLHAV RAHLHFTTGR 300
PEERLTFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLIAK EVGTLTRAFS 350
AKLEAEHFKN EPKGISRFLP GARPKRKALD VEGFYEDGGR LNIEGQEIFE 400
ADPVNLIRLF KIADERDLDL HPDAFTAVTR ALPLITSRVR RDPDACRAFL 450
DLLARGKRSY RTLTLMNDAG VLGRFIPEFG RVVAQMQFNM YHSYTVDEHT 500
LRAVGVIGDI AAGRLVDDHP LAVSIMPLIE DREALFLAML LHDTGKGGVG 550
GQEKAGARSA RSACERLGVE RSKVELVAWL VENHLVMSDF AQKRDVSDPG 600
TVAAFARIVE NPERLRLLLV ITVADIRAVG PGVWNGWKGQ LLRELYNATE 650
AVFRGGRGSD AAANVQRHQE STAEAARAAL LETDPAAKGW VAAMENAYFS 700
AFSQDDLFHH AELARRAAIQ GGAAAEGQVR PGSNAAEVVI AAKDRRGLFA 750
DLALAISSLG GNVVGARVFT SRQGQALDVF YVQDVTGAPF GCENPRALRR 800
LADALEAAGK GDALAVEPRR GSEQTRAAAF AIAPSVTIDN DASNDATVVE 850
ASGRDRPGLL HALAKTLADS ALSIQSAHID GYGERAVDAF YVQTTEGGKV 900
TDTRKLNALK ADLLAALEQN EASAPAARPG LRRARASVAR 940
Length:940
Mass (Da):103,396
Last modified:March 3, 2009 - v1
Checksum:i2F1985420353F8ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001340 Genomic DNA. Translation: ACL93480.1.
RefSeqiWP_010917903.1. NC_011916.1.
YP_002515388.1. NC_011916.1.

Genome annotation databases

EnsemblBacteriaiACL93480; ACL93480; CCNA_00013.
GeneIDi7332895.
KEGGiccs:CCNA_00013.
PATRICi21304593. VBICauCre52860_0014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001340 Genomic DNA. Translation: ACL93480.1 .
RefSeqi WP_010917903.1. NC_011916.1.
YP_002515388.1. NC_011916.1.

3D structure databases

ProteinModelPortali B8GWX0.
SMRi B8GWX0. Positions 386-632.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 190650.CC_0013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL93480 ; ACL93480 ; CCNA_00013 .
GeneIDi 7332895.
KEGGi ccs:CCNA_00013.
PATRICi 21304593. VBICauCre52860_0014.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci CAULONA1000:CCNA_00013-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.
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. "The genetic basis of laboratory adaptation in Caulobacter crescentus."
    Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
    J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NA1000 / CB15N.

Entry informationi

Entry nameiGLND_CAUCN
AccessioniPrimary (citable) accession number: B8GWX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 43 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

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