Reviewed, UniProtKB/Swiss-Prot A3M4Q8 (GLND_ACIBT)

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:	A1S_1474

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	887 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 – 887	887	[Protein-PII] uridylyltransferase HAMAP MF_00277		PRO_1000114748

Sequences

	Sequence		Length	Mass (Da)
	A3M4Q8-1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 5D8D5FB823A833F9	FASTA	887	102,126
	10 20 30 40 50 60 MINTSPLLNY VSSHHDIKAI NQWRTDVEKQ LQDSYENGQS IREIIKARSD LVDEALVFLW 70 80 90 100 110 120 KHAELDQSKL GLFAVGGYGR REMLPYSDVD IMILSEDEIS EENEKRISTF ISSLWDVGNF 130 140 150 160 170 180 KPGISVRTIQ SCVEQAATDL TVATTLIEAR LITGNTQLAK WPRRIVSQTW TDKTFYDAKM 190 200 210 220 230 240 AEQAKRYHQH NNTESNLEPD IKNAPGGIRD INQIGWIAKR HFRVNRIYDL VHLGFISEFE 250 260 270 280 290 300 LAVLEEAESF LWEIRHHLHR LAKRDENRLL FDHQREIAAK FGYVRQEGQP VNYGVEQFMK 310 320 330 340 350 360 RYYRTAQQVS TLNEMLLAYF SESVITPRLP NYERKIEVVN DHFKIVDNKL AVQHHKIFAE 370 380 390 400 410 420 HPSAILELFY ILANRPDIEG IRARTLRLLI LAAKRINQSY RDNPEHQALF MSIIRSPYRL 430 440 450 460 470 480 YDTLVAMKRY GVLGNYIPAF GQIMGLMQYD LFHIYTVDAH TLLLLRNLNR FREPEFAKEF 490 500 510 520 530 540 PVVSSVFQRL ARQDIVFIAA LFHDIAKGRG GDHSELGAED AIEFGRAHGF TERECKLIAW 550 560 570 580 590 600 LIQNHLLMSL TAQKKDISDP DVVKDFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 610 620 630 640 650 660 SLMRQLYTHA RDVIRTGLGR PVDYQMLIED TKFAASELLV NNFALADVEK VWQELGDEYF 670 680 690 700 710 720 IKESADEIAW HTQAILKHGD NPEPLVLLRA HRKAAQDAVQ IFIYTRDQPN LFATTVAVLD 730 740 750 760 770 780 RMNLDVQDAK IITASTAFSL DTYVVLDRFG TLLTDPEREE TVKNALVKAL SQPDQYPGLM 790 800 810 820 830 840 QRRIPRQLRH FDIENTVDVT LNEALQQNMV EISTLDHPGL LARVGGLFMM QGLDIHSARI 850 860 870 880 ATLGERAEDI FFVTKKDGKP LNHEEVKLFS EKLKAALDEA SNQICQH

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000521 Genomic DNA. Translation: ABO11902.2.
RefSeq	YP_001084504.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A3M4Q8.
Genome annotation databases
GeneID	4917458.
GenomeReviews	Gene locus A1S_1474 in contig CP000521_GR.
KEGG	acb:A1S_1474.
NMPDR	fig|400667.4.peg.1527.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2844.
HOGENOM	HBG687872.
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_ACIBT

Accession

Primary (citable) accession number: A3M4Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 2, 2008
Last modified:	February 9, 2010
This is version 26 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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