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Reviewed, UniProtKB/Swiss-Prot P27249 (GLND_ECOLI)

Last modified June 16, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    [Protein-PII] uridylyltransferase
      Short name=PII uridylyl-transferase
    EC=2.7.7.59
Alternative name(s):
    Uridylyl-removing enzyme
    UTase
Gene names
Name: glnD
Ordered Locus Names: b0167, JW0162
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length890 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Modifies, by uridylylation or deuridylylation the PII (glnB) regulatory protein. HAMAP MF_00277

Catalytic activity

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

Sequence similarities

Belongs to the glnD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 890890[Protein-PII] uridylyltransferase HAMAP MF_00277
PRO_0000192732

Experimental info

Sequence conflict471L → S in AAA23878. Ref.1
Sequence conflict2251G → A Ref.3
Sequence conflict357 – 3582RG → TR in AAA23878. Ref.1
Sequence conflict5231D → H in AAA23878. Ref.1
Sequence conflict7031A → R in CAA79887. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P27249-1 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 6FF0006341A71D34

FASTA890102,390
        10         20         30         40         50         60 
MNTLPEQYAN TALPTLPGQP QNPCVWPRDE LTVGGIKAHI DTFQRWLGDA FDNGISAEQL 

        70         80         90        100        110        120 
IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL HPLSDVDLLI LSRKKLPDDQ 

       130        140        150        160        170        180 
AQKVGELLTL LWDVKLEVGH SVRTLEECML EGLSDLTVAT NLIESRLLIG DVALFLELQK 

       190        200        210        220        230        240 
HIFSEGFWPS DKFYAAKVEE QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF 

       250        260        270        280        290        300 
GATSLDEMVG FGFLTSAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 

       310        320        330        340        350        360 
YSGEGNEPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPI DDEFQLRGTL 

       370        380        390        400        410        420 
IDLRDETLFM RQPEAILRMF YTMVHNSAIT GIYSTTLRQL RHARRHLQQP LCNIPEARKL 

       430        440        450        460        470        480 
FLSILRHPGA VRRGLLPMHR HSVLGAYMPQ WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE 

       490        500        510        520        530        540 
SFASEETRQR HPLCVDVWPR LPSTELIFIA ALFHDIAKGR GGDHSILGAQ DVVHFAELHG 

       550        560        570        580        590        600 
LNSRETQLVA WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTENRLRYL VCLTVADICA 

       610        620        630        640        650        660 
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL RMDNIDEEAL 

       670        680        690        700        710        720 
HQIWSRCRAN YFVRHSPNQL AWHARHLLQH DLSKPLVLLS PQATRGGTEI FIWSPDRPYL 

       730        740        750        760        770        780 
FAAVCAELDR RNLSVHDAQI FTTRDGMAMD TFIVLEPDGN PLSADRHEVI RFGLEQVLTQ 

       790        800        810        820        830        840 
SSWQPPQPRR QPAKLRHFTV ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI 

       850        860        870        880        890 
SLHGARITTI GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of gldD, the gene for uridylyl transferase and uridyl removing enzyme of E. coli."
Park S.-C., Kim I.H., Rhee S.G.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."
van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.
Mol. Microbiol. 9:443-458(1993) [PubMed: 8412694] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases

M96431 Genomic DNA. Translation: AAA23878.1.
Z21842 Genomic DNA. Translation: CAA79887.1.
U70214 Genomic DNA. Translation: AAB08596.1.
U00096 Genomic DNA. Translation: AAC73278.1.
AP009048 Genomic DNA. Translation: BAE76045.1.
PIRG64740.
RefSeqAP_000827.1.
NP_414709.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9779N.
IntActP27249. 23 interactions.

Genome annotation databases

GeneID944863.
GenomeReviewsGene locus JW0162 in contig AP009048_GR.
Gene locus b0167 in contig U00096_GR.
KEGGecj:JW0162.
eco:b0167.

Organism-specific databases

EchoBASEEB1383.
EcoGeneEG11411. glnD.
CMRSearch...

Phylogenomic databases

HOGENOMP27249.
OMAP27249. MQHDLFH.

Enzyme and pathway databases

BioCycEcoCyc:GLND-MON.
BRENDA2.7.7.59. 246.

Family and domain databases

HAMAPMF_00277.
[Tree]
InterProIPR002912. ACT_bd.
IPR010043. GlnD_Uridyltrans.
IPR003607. Met-dep_phosphohydro_HD.
IPR006674. Met-dep_phosphohydro_HD_sub.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. GlnD_Uridyltrans. 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.
ProtoNetSearch...

Entry information

Entry nameGLND_ECOLI
AccessionPrimary (citable) accession number: P27249
Secondary accession number(s): Q2MCG1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents