Reviewed, UniProtKB/Swiss-Prot B7N834 (GLND_ECOLU)

Names and origin

Protein names

Recommended 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:	ECUMN_0163

Organism

Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585056 [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 By similarity. HAMAP MF_00277
Catalytic activity	UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP MF_00277
Sequence similarities	Belongs to the glnD family.

Ontologies

Keywords
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	[protein-PII] uridylyltransferase activity Inferred from electronic annotation. Source: HAMAP amino acid binding 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 MF_00277		PRO_1000119365

Sequences

	Sequence		Length	Mass (Da)
	B7N834-1 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 84FA68FA7ABBD388	FASTA	890	102,414
	10 20 30 40 50 60 MNTLPEQYAN TALPTLPGQP QNPCAWPRDE LTVCGIKAHI DTFQRWLGDA FDNGISAEQL 70 80 90 100 110 120 IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL HPLSDIDLLI 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 YTMVRNSAIT 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 TFIVLEPDGS PLSADRHEVI RFGLEQVLTQ 790 800 810 820 830 840 SSWQPPQPRR QPAKLRHFTV ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI 850 860 870 880 890 SLHGARITTI GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928163 Genomic DNA. Translation: CAR11384.1.
RefSeq	YP_002410940.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7156109.
GenomeReviews	Gene locus ECUMN_0163 in contig CU928163_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG687872.
OMA	MQHDLFH.
Family and domain databases
HAMAP	MF_00277. PII_uridylyl-transf. [Tree]
InterPro	IPR002912. ACT_bd. IPR010043. GlnD_Uridyltrans. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR006674. Metal-dep_PHydrolase_HD_sub. IPR002934. Nucleotidyltransferase. IPR013546. PII_UdlTrfase/GS_AdlTrfase. [Graphical view]
PANTHER	PTHR13734:SF1. GlnD_Uridyltrans. 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_ECOLU

Accession

Primary (citable) accession number: B7N834

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	February 9, 2010
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)