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Q5QXT0 (GLND_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
[Protein-PII] uridylyltransferase

Short name=PII uridylyl-transferase
EC=2.7.7.59
Alternative name(s):
UTase
Uridylyl-removing enzyme
Gene names
Name:glnD
Ordered Locus Names:IL0847
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies, by uridylylation or deuridylylation the PII (GlnB) regulatory protein By similarity. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 879879[Protein-PII] uridylyltransferase HAMAP-Rule MF_00277
PRO_0000192738

Sequences

Sequence LengthMass (Da)Tools
Q5QXT0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 7DFEC2D5EA90098B

FASTA879101,332
        10         20         30         40         50         60 
MANVQEDKDF HGRWPDRTLQ PCLKDYKALL ESYQNWSAAR FVTADIDELV HHRATFFDQL 

        70         80         90        100        110        120 
ISQLWQQFQL EDEPASILAV GGYGRETLHP GSDIDLLILV GPENAEAEAK LSEKLGQFVT 

       130        140        150        160        170        180 
FLWDLHLDIG HSVRTIEDCF AQSENDITIA TNLIESRYLS GAESLYNEFH QQLLNDFPWS 

       190        200        210        220        230        240 
SRDFYQAKLD EQKQRHQQYH STSYNLEPNI KSSPGGLRDI QTVGWIAKRH FRTHSDENLV 

       250        260        270        280        290        300 
EYGYMTADEF VELRDCMNWL WRIRFALHLE AGKREDRLLF DFQPGVAVRL GYGNDGKASV 

       310        320        330        340        350        360 
ETMMKDYFKV VLRVSELNQM LLQFFHQAIL GTQDLQHAEH ISDDFAVANK LLTARHDNVF 

       370        380        390        400        410        420 
DNHCNIIRAF VCIAEHPQIQ GIHSNTIRLL RNARAQLSEP LSHDPECRDL FNQLIQHPRG 

       430        440        450        460        470        480 
CGLSFALMHH HSVLASYLSQ WQQIVGQMQF DLFHAYTVDE HTFRLVRNLY RFSDEDYQDQ 

       490        500        510        520        530        540 
FPLCEKLVAQ MDRRYCLYLA GIFHDIAKGR GGDHSELGEM DARNFCHQHG YSEEDAELVA 

       550        560        570        580        590        600 
WLVRHHLTMS VTAQKRDIHD PEVIQDFANQ VSTPERLDYL YCLTVADIRA TNQSLWNNWK 

       610        620        630        640        650        660 
ATLLEELYNA TSYLLQQDSN KPTLDIRQKI NENKASAMAL LLSAGFEKAE ILALWGRFTA 

       670        680        690        700        710        720 
DYFFRHTAEQ ISWHSQHILN LPSEQLPLIL IGDENNYGTT ELFIYHHEEG HLFASVAGVL 

       730        740        750        760        770        780 
DSQQLNILDA QILATRDGFV MDTFVVLQRD GKPLTEPHRI EEVKQQLLDV LHKRIPVPST 

       790        800        810        820        830        840 
KRPLSRRMKN FSVATEVTFI PSKHHGRTTF ELVTLDRPGL IAKLAAILQQ QNVILLAAKI 

       850        860        870 
TTIGEQAEDL FIVTTEQQTA LSDKQKKTLK AKIIKDLEF 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81687.1.
RefSeqYP_155236.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXT0.
ModBaseSearch...

Protein-protein interaction databases

STRING283942.IL0847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81687; AAV81687; IL0847.
GeneID3173614.
KEGGilo:IL0847.
PATRIC22139727. VBIIdiLoi21852_0849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.

Enzyme and pathway databases

BioCycILOI283942:GI0U-880-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl-transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLND_IDILO
AccessionPrimary (citable) accession number: Q5QXT0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 4, 2005
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families