[Protein-PII] uridylyltransferase - Escherichia coli (strain K12)

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P27249 (GLND_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
[Protein-PII] uridylyltransferase
Short name=PII uridylyl-transferase
EC=2.7.7.59

Alternative name(s):
UTase
Uridylyl-removing enzyme

Gene names

Name:	glnD
Ordered Locus Names:	b0167, JW0162

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Modifies, by uridylylation or deuridylylation the PII (GlnB) regulatory protein. HAMAP-Rule MF_00277
Catalytic activity	UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277
Sequence similarities	Belongs to the GlnD family.

Ontologies

Keywords
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from direct assay PubMed 6130097. Source: EcoCyc nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	[protein-PII] uridylyltransferase activity Inferred from direct assay PubMed 6130097. Source: EcoCyc amino acid binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: InterPro phosphoric diester hydrolase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 890

890

[Protein-PII] uridylyltransferase HAMAP-Rule MF_00277

PRO_0000192732

Experimental info

Sequence conflict

L → S in AAA23878. Ref.1

Sequence conflict

225

G → A Ref.3

Sequence conflict

357 – 358

RG → TR in AAA23878. Ref.1

Sequence conflict

523

D → H in AAA23878. Ref.1

Sequence conflict

703

A → R in CAA79887. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P27249 [UniParc].

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

890

102,390

        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' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	G64740.
RefSeq	NP_414709.1. NC_000913.2. YP_488469.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P27249.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9779N.
IntAct	P27249. 23 interactions.
MINT	MINT-1252261.
STRING	511145.b0167.
Proteomic databases
PaxDb	P27249.
PRIDE	P27249.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73278; AAC73278; b0167. BAE76045; BAE76045; BAE76045.
GeneID	12930753. 944863.
KEGG	ecj:Y75_p0163. eco:b0167.
PATRIC	32115441. VBIEscCol129921_0172.
Organism-specific databases
EchoBASE	EB1383.
EcoGene	EG11411. glnD.
Phylogenomic databases
eggNOG	COG2844.
HOGENOM	HOG000261778.
KO	K00990.
OMA	SPKVWNA.
ProtClustDB	PRK05007.
Enzyme and pathway databases
BioCyc	EcoCyc:GLND-MONOMER. ECOL316407:JW0162-MONOMER. MetaCyc:GLND-MONOMER.
BRENDA	2.7.7.59. 2026.
SABIO-RK	P27249.
Gene expression databases
Genevestigator	P27249.
Family and domain databases
Gene3D	1.10.3210.10. 1 hit.
HAMAP	MF_00277. PII_uridylyl-transf.
InterPro	IPR002912. ACT_dom. IPR010043. GlnD_Uridyltrans. IPR003607. HD/PDEase_dom. IPR006674. HD_domain. IPR002934. Nucleotidyltransferase. IPR013546. PII_UdlTrfase/GS_AdlTrfase. [Graphical view]
PANTHER	PTHR13734:SF1. PTHR13734:SF1. 1 hit.
Pfam	PF01842. ACT. 2 hits. PF08335. GlnD_UR_UTase. 1 hit. PF01966. HD. 1 hit. PF01909. NTP_transf_2. 1 hit. [Graphical view]
PIRSF	PIRSF006288. PII_uridyltransf. 1 hit.
SMART	SM00471. HDc. 1 hit. [Graphical view]
TIGRFAMs	TIGR01693. UTase_glnD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLND_ECOLI

Accession

Primary (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:	May 29, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents