Reviewed, UniProtKB/Swiss-Prot Q63T10 (GLND_BURPS)

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:	BPSL2161

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	858 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 – 858	858	[Protein-PII] uridylyltransferase HAMAP MF_00277		PRO_0000192726

Sequences

	Sequence		Length	Mass (Da)
	Q63T10-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 56A684E5D8C9D1AC	FASTA	858	96,711
	10 20 30 40 50 60 MSASVAEPPP ALSRKAEFKA AKAELLARFK SANHVTPLMH ALSRATDDAL RSLWQECGLP 70 80 90 100 110 120 ATLALVAVGG FGRGELSPHS DVDILVLLPD AHASELDERI ERFIGMAWDL GLEIGSSVRT 130 140 150 160 170 180 VGQCIEEASH DVTVQTSLLE ARRIVGSTAL FERFMLRYRE ALDARAFFQA KVLEMRQRHA 190 200 210 220 230 240 KFQDTPYSLE PNVKESPGGL RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE 250 260 270 280 290 300 GFLKTLRARL HVIAGRRQDI LVFDLQTQAA ESFGYQPTSA KRASEQLMRR YYWAAKAVTQ 310 320 330 340 350 360 LATILIQNIE AQLFPATSGV TRVLSPGRFV EKQGMLEIAA DDVFERHPDA ILEAFLLYEA 370 380 390 400 410 420 TRGVKGLSAR TLRALYNSRD VMNNAWRRDP RNRRTFMQIL QQPEGITHAF RLMNQTSVLG 430 440 450 460 470 480 RYLLNFRRIV GQMQHDLYHV YTVDQHILMV LRNIRRFAVA EHAHEYPFCS QLIVNFERPW 490 500 510 520 530 540 VLYVAALFHD IAKGRGGDHS ALGMADARRF CREHGIEGDD AALVVWLVQH HLTMSQVAQK 550 560 570 580 590 600 QDTSDPVVIK RFAELVGSER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL 610 620 630 640 650 660 GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA DIAWQTRVLY 670 680 690 700 710 720 RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY FDRNGLSVLD ARVNTTRHGY 730 740 750 760 770 780 ALDNFIVTQT EHDVQYRDIA NLVEQQLAAR LAESAPLPEP SKGRLSRLSR TFPITPRVDL 790 800 810 820 830 840 RADERGQYYI LSVSANDRPG LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS 850 DNRLQIQVET ELLRAIAV

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH36163.1.
RefSeq	YP_108756.1.
3D structure databases
SMR	Q63T10. Positions 51-301, 680-838.
ModBase	Search...
Genome annotation databases
GeneID	3093139.
GenomeReviews	Gene locus BPSL2161 in contig BX571965_GR.
KEGG	bps:BPSL2161.
NMPDR	fig|272560.3.peg.4480.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG687872.
OMA	MQHDLFH.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL2161-MONOMER.
BRENDA	2.7.7.59. 275934.
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. 1 hit. 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_BURPS

Accession

Primary (citable) accession number: Q63T10

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	October 25, 2004
Last modified:	February 9, 2010
This is version 36 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)