Reviewed, UniProtKB/Swiss-Prot Q6FAM5 (GLND_ACIAD)

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:	ACIAD2079

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	888 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 – 888	888	[Protein-PII] uridylyltransferase HAMAP MF_00277		PRO_0000192713

Sequences

	Sequence		Length	Mass (Da)
	Q6FAM5-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 1F244D77538E36FC	FASTA	888	102,208
	10 20 30 40 50 60 MIITSPLLDY VTSHQDIKAI NQWRADVEQQ LQEFYENGYS IRDIVLARSN LIDEALTFLW 70 80 90 100 110 120 KHAGLDQSDL GLFAVGGYGR REMLPYSDVD IMILSENDIS PEHEKQISGF ISSLWDVGNF 130 140 150 160 170 180 KPGTSVRSIQ NCVEQATNDL TVATTLIESR LITGNPDLAK WPRRIVSQTW TDKTFFDAKM 190 200 210 220 230 240 EEQAKRHAQH NNTESNLEPD IKNAPGGIRD MNQIGWIAKR HFRVNRIYDL VHLGFITEYE 250 260 270 280 290 300 LKVLEEAESF LWEIRHHLHL LSKRDENRLL FDHQREIAAK FGYTRAEGQP VNFAVEQFMK 310 320 330 340 350 360 RYYRTAQQVS TLNEMLLAYF NESVITPRLP NYERKIEEIN ENFKLVDGKL AVQHHKVFSE 370 380 390 400 410 420 NPSAILELFY LLANHPEIEG IRARTLRLLI MAAKRIDQEF RDNPAHQALF MAIIRSPYRL 430 440 450 460 470 480 YDTLVDMKRY GILGNYIPAF GQIMGLMQYD LFHIYTVDAH TLLLIRNLNR FKEPEFAQHF 490 500 510 520 530 540 PVVSSVFQRL ARRDIVYLAA IFHDIAKGRG GDHSELGAED AIEFCRAHGF TERECKLVAW 550 560 570 580 590 600 LIHNHLLMSL TAQKKDISDP DVIKEFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 610 620 630 640 650 660 SLMRQLYTYS RDVIRSGLGR PVDYQMLIED TKFSASETLV NEFSLDAVEK VWQELGDEYF 670 680 690 700 710 720 LKESADEIAW HTRAILQHGD NPAPIVLLRA HRQSAQDAVQ IFIYTQDKPN LFATTVAVLD 730 740 750 760 770 780 RMNLDVQDAR IITATKAFSL DTYVVLDRFG TLLTDPEREH TVKEALIKAL SQSDKYPGLM 790 800 810 820 830 840 QRRIPRQLRH FDIENTVDIT LNPVLQQNMV EISTLDQPGL LARVGGLFMM QGLDIHSAKI 850 860 870 880 ATLGERAEDI FFVTKKDGQP MTTDEAHIFS AQLKLALDEA SNQIVSQH

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG68888.1.
RefSeq	YP_046710.1.
3D structure databases
SMR	Q6FAM5. Positions 39-314, 449-547, 700-854.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FAM5.
Genome annotation databases
GeneID	2881141.
GenomeReviews	Gene locus ACIAD2079 in contig CR543861_GR.
KEGG	aci:ACIAD2079.
NMPDR	fig|62977.3.peg.1972.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2844.
HOGENOM	HBG687872.
OMA	MQHDLFH.
PhylomeDB	Q6FAM5.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD2079-MONOMER.
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_ACIAD

Accession

Primary (citable) accession number: Q6FAM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 38 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)