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C7C6X7 (C7C6X7_METED) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277

Short name=UTase/UR HAMAP-Rule MF_00277
Alternative name(s):
Bifunctional [protein-PII] modification enzyme HAMAP-Rule MF_00277
Bifunctional nitrogen sensor protein HAMAP-Rule MF_00277
Gene names
Name:glnD HAMAP-Rule MF_00277 EMBL CAX21881.1
Ordered Locus Names:METDI0212 EMBL CAX21881.1
OrganismMethylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium dichloromethanicum (strain DM4)) [Complete proteome] [HAMAP] EMBL CAX21881.1
Taxonomic identifier661410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length928 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277 SAAS SAAS013546

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277 SAAS SAAS013546

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277 SAAS SAAS013546

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

Domain

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. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family. HAMAP-Rule MF_00277

Contains 1 HD domain. HAMAP-Rule MF_00277

Contains 2 ACT domains. HAMAP-Rule MF_00277

Contains ACT domains. SAAS SAAS013546

Contains HD domain. SAAS SAAS013546

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain510 – 614105HD By similarity HAMAP-Rule MF_00277
Domain725 – 80278ACT 1 By similarity HAMAP-Rule MF_00277
Domain835 – 91884ACT 2 By similarity HAMAP-Rule MF_00277
Region1 – 367367Uridylyltransferase By similarity HAMAP-Rule MF_00277
Region369 – 724356Uridylyl-removing By similarity HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
C7C6X7 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: D3C1E4F56083055A

FASTA928104,425
        10         20         30         40         50         60 
MFDPVPVLEK IVASLDRDAR EPTKLRGLLV PELRKVIETG HAEAERLLLK ERDGLACAQR 

        70         80         90        100        110        120 
LSRLTDAVVR AIYDAVVWRL YPNDNPSTGE HLAIVATGGY GRGTMAPGSD IDLLFLLPYK 

       130        140        150        160        170        180 
QTAWSESVVE AMLYVLWDLK LKVGHATRSV EECLREGRAD MTIRTALLES RFLFGSRSLF 

       190        200        210        220        230        240 
EEMVTRFDTE LVIGSASEFV DAKLRERDAR VAKAGASRYL VEPNVKDGKG GLRDLNTLFW 

       250        260        270        280        290        300 
IAKYTYRVRN QAELVHAGLF TPDEYRLFER CEEFLWRVRC HIHFVTGRPE ERLSFGLQPK 

       310        320        330        340        350        360 
IAERLGFGSR GGLSGVERFM KAYFLIAKDV GDLTAIVCAE LEARHAKRTP VLDRWIGRFR 

       370        380        390        400        410        420 
DRFRATSIEA EDFWIDNGRV NIRGEDAFER DPVNLIRLFW LADRHNLPIH PDAARLANRS 

       430        440        450        460        470        480 
LKLITHAVRI DPEANRLFLD ILTSKNAPET ILRSMNEAGV LGRFIPEFGR IVAMMQFNMY 

       490        500        510        520        530        540 
HHYTVDEHLL RSLGVLAAID SGRVRDEHPL ASRLIDTIHN RRALYVAILL HDIAKGRPED 

       550        560        570        580        590        600 
HSIAGAAIAR KLGPRFGLSQ AETETVSWLV EHHLLMSMTA QSRDLSDRRT IEKFASEVQS 

       610        620        630        640        650        660 
LERLKLLAIL TVADIKAVGP GVWTAWKGTL LRTLYDETEV VLSGGHSEIA RTDRVRLIQM 

       670        680        690        700        710        720 
ALREQLSDWN SELFDGYAAR HNQAYWLKVD STRHFKNARF LRTVMEEGRT SATTYETDPV 

       730        740        750        760        770        780 
RGVTELTVYS PDHPRLLAII TGACATMGGN IVDAQIFTTT DGFALDSIFI SRAFERDEDE 

       790        800        810        820        830        840 
LRRAGRIATA IERALKGEIK IAELVADKHP KQPPKTFLVP PDVSIDNALS SRETVVEITG 

       850        860        870        880        890        900 
LDRPGLLYEL TTGLNRLSLN ITSAHVATFG ERAVDVFYVT DLTGTRVVQP DRLAMIRAAV 

       910        920 
MEVFASDVAA LRAEGLDALV DSPPPREL 

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References

[1]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. expand/collapse author list , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E.
PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5838 / DM4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FP103042 Genomic DNA. Translation: CAX21881.1.
RefSeqYP_003065946.1. NC_012988.1.

3D structure databases

ProteinModelPortalC7C6X7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING661410.METDI0212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAX21881; CAX21881; METDI0212.
GeneID8190687.
KEGGmdi:METDI0212.
PATRIC22519508. VBIMetExt143287_0329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05092.

Enzyme and pathway databases

BioCycMEXT661410:GJA1-205-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC7C6X7_METED
AccessionPrimary (citable) accession number: C7C6X7
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)