C8U1N5 (C8U1N5_ECO10) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
[Protein-PII] uridylyltransferase HAMAP MF_00277
Short name=PII uridylyl-transferase HAMAP MF_00277
EC=2.7.7.59 HAMAP MF_00277

Alternative name(s):
UTase HAMAP MF_00277
Uridylyl-removing enzyme HAMAP MF_00277

Gene names

Name:	glnD HAMAP MF_00277 EMBL BAI29043.1
Ordered Locus Names:	ECO103_0165

Organism

Escherichia coli O103:H2 (strain 12009 / EHEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585395 [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 SAAS SAAS002912
Catalytic activity	UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP MF_00277 SAAS SAAS002912
Sequence similarities	Belongs to the glnD family. HAMAP MF_00277

Ontologies

Keywords
Molecular function	Nucleotidyltransferase HAMAP MF_00277 SAAS SAAS002912 EMBL BAI29043.1 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 metal ion binding Inferred from electronic annotation. Source: InterPro phosphoric diester hydrolase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	C8U1N5 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: 66FE695C1E245428	FASTA	890	102,396
	10 20 30 40 50 60 MNTLPEQYAN TALPTLPGQP QNPCVWPRDE LTVGGIKAHI 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]

"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli." Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T. Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed: 19815525] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 12009 EMBL BAI29043.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP010958 Genomic DNA. Translation: BAI29043.1.
RefSeq	YP_003220177.1. NC_013353.1.
3D structure databases
ProteinModelPortal	C8U1N5.
SMR	C8U1N5. Positions 469-599.
ModBase	Search...
Protein-protein interaction databases
STRING	C8U1N5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000180133; EBESCP00000169060; EBESCG00000178033.
GeneID	8475028.
GenomeReviews	Gene locus ECO103_0165 in contig AP010958_GR.
KEGG	eoh:ECO103_0165.
PATRIC	32091871. VBIEscCol146794_0170.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009422.
OMA	MQHDLFH.
ProtClustDB	PRK05007.
Family and domain databases
HAMAP	MF_00277. PII_uridylyl_transf. [Tree]
InterPro	IPR002912. ACT-bd. IPR010043. GlnD_Uridyltrans. IPR023279. HD. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR006674. Metal-dep_PHydrolase_HD_sub. IPR002934. Nucleotidyltransferase. IPR013546. PII_UdlTrfase/GS_AdlTrfase. [Graphical view]
Gene3D	G3DSA:1.10.3210.10. HD. 1 hit.
KO	K00990.
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

C8U1N5_ECO10

Accession

Primary (citable) accession number: C8U1N5

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)