[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Park S.-C., Kim I.H., Rhee S.G.; "Molecular cloning and sequencing of gldD, the gene for uridylyl transferase and uridyl removing enzyme of E. coli."; Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; PubMed=8412694 [NCBI, ExPASy, EBI, Israel, Japan] van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.; "The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."; Mol. Microbiol. 9:443-458(1993).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/nar/22.9.1637; PubMed=8202364 [NCBI, ExPASy, EBI, Israel, Japan] Fujita N., Mori H., Yura T., Ishihama A.; "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."; Nucleic Acids Res. 22:1637-1639(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; 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.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

FUNCTION: Modifies, by uridylylation or deuridylylation the PII (glnB) regulatory protein.
CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].
SIMILARITY: Belongs to the glnD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M96431; AAA23878.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z21842; CAA79887.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U70214; AAB08596.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73278.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76045.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G64740; G64740.

RefSeq

AP_000827.1; -.
NP_414709.1; -.

3D structure databases

ModBase

P27249.

Protein-protein interaction databases

DIP

DIP:9779N; -.

IntAct

P27249; -.

Enzyme and pathway databases

BioCyc

EcoCyc:GLND-MON; -.

Organism-specific databases

EchoBASE

EB1383; -.

EcoGene

EG11411; glnD.

Ontologies

GO:0008773;	Molecular function: [protein-PII] uridylyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0016597;	Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0006807;	Biological process: nitrogen compound metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00277; -; 1.
PBIL [Tree]

InterPro

IPR002912; ACT_bd.
IPR013546; GlnD_UR_UTase.
IPR010043; GlnD_Uridyltrans.
IPR003607; Met-dep_phosphohydro_HD.
IPR006674; Met-dep_phosphohydro_HD_sub.
IPR002934; Nucleotidyltransferase.
Graphical view of domain structure.

PANTHER

PTHR13734:SF1; GlnD_Uridyltrans; 1.

Pfam

PF01842; ACT; 2.
PF08335; GlnD_UR_UTase; 1.
PF01966; HD; 1.
PF01909; NTP_transf_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF006288; PII_uridyltransf; 1.

SMART

SM00471; HDc; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR01693; UTase_glnD; 1.

Genome annotation databases

GeneID

944863; -.

GenomeReviews

U00096_GR; b0167.
AP009048_GR; JW0162.

KEGG

ecj:JW0162; -.
eco:b0167; -.

Phylogenomic databases

HOGENOM

P27249; -.

Genome annotation databases

CMR

P27249; b0167.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 890`	`890`	`[Protein-PII] uridylyltransferase.`	`PRO_0000192732`
`CONFLICT`	`47 47`		`L -> S (in Ref. 1; AAA23878).`
`CONFLICT`	`225 225`		`G -> A (in Ref. 3).`
`CONFLICT`	`357 358`		`RG -> TR (in Ref. 1; AAA23878).`
`CONFLICT`	`523 523`		`D -> H (in Ref. 1; AAA23878).`
`CONFLICT`	`703 703`		`A -> R (in Ref. 2; CAA79887).`

Sequence information

Length: 890 AA [This is the length of the unprocessed precursor]

Molecular weight: 102390 Da [This is the MW of the unprocessed precursor]

CRC64: 6FF0006341A71D34 [This is a checksum on the sequence]

        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

P27249 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools