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Reviewed, UniProtKB/Swiss-Prot Q8RQD1 (GLND_AZOBR)

Last modified February 9, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Modifies, by uridylylation or deuridylylation the PII (glnB) regulatory protein. HAMAP MF_00277

Catalytic activity

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

Sequence similarities

Belongs to the glnD family.

Ontologies

Keywords
   Biological processNitrogen fixation
   Molecular functionNucleotidyltransferase
Transferase
Gene Ontology (GO)
   Biological processnitrogen fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933[Protein-PII] uridylyltransferase HAMAP MF_00277
PRO_0000192716

Sequences

Sequence LengthMass (Da)Tools
Q8RQD1-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 35E692E0411BB9E7

FASTA933104,602
        10         20         30         40         50         60 
MLSTRAASAD ASDAKDAGTA NIPNKRAILS RRKLAEDLET LVAEHGTGDK LRPALIARLR 

        70         80         90        100        110        120 
GALNDGRAEV RARFEAKGSG EDCVRQNCYL ADGVVRSLAD LTVTHIFPTP NPTSGEVFDI 

       130        140        150        160        170        180 
VATGGYGRGE LAPFSDIDLL FLLPYKRTPR VEQVVEYMLY ILWDLGLKVG HAVRSVDDCI 

       190        200        210        220        230        240 
RQSKADVTIR TAILESRYLW GPRKLFHRLR RRFDREVVAG TGPEFVEAKL AERDNRHLKL 

       250        260        270        280        290        300 
GDSAYVLEPN LKDGKGGLRD LQTLFWIAKY LYRVEDVDDL VGKKVLLPEE AHGFAKAQNF 

       310        320        330        340        350        360 
LWTARCHLHY LTGRMEDRMT FDVQTSIGNR MGYTDHAGTK GVERFMKHYF LVAKDVGDLT 

       370        380        390        400        410        420 
RIFCAALEAE SKRPPKFNIL RLAALARRKD VDGFVVDGER LNVRSDRQFK DEPLDMIRLF 

       430        440        450        460        470        480 
HTAQQNDIDI HPNALRAITR SLSVVGPKLR ADPEANRLFL EILTGRKDPE ITLRRMNEAG 

       490        500        510        520        530        540 
VLARFIPDFG RVVAQMQYDM YHVYTVDEHT LFALGILHKI EMGELTDELP LSSEVIHKVV 

       550        560        570        580        590        600 
SRRALYVAVL LHDIAKGRGG DHSILGARVA EKLCPRLGLT AEETETVAWL VRWHLAMSYT 

       610        620        630        640        650        660 
AFKRDLEDDK TVRDFVSLVQ SPERLRLLLV LTVADIRAVG PQRWNNWKAT LLRELYNRSE 

       670        680        690        700        710        720 
EVMSGGLSVE GRGRRIQAAQ AALRDELSDF DAADFERHLA LGYPAYWLAF DAETLGRQAR 

       730        740        750        760        770        780 
LVRGRLRDER PLTVNTRIDR GRAITEVTIF ATDHHGLFSR LAGALAAAGA DIVDARIFTM 

       790        800        810        820        830        840 
TNGMALDVFT VQDAAGGGAF ESGDKLAKLS VMIEKVLSGQ LKPLHDLTKR KAPHASRTRV 

       850        860        870        880        890        900 
FHVPPRVLID NNASTTHTVI EVNGRDRPGL LYDLTRALTN LTLQISSAKI STYGEKAIDV 

       910        920        930 
FYVKDVFGLK VTHENKLAQI RERLLHALAD PSA 

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References

[1]"Cloning and characterization of the Azospirillum brasilense glnD gene and analysis of a glnD mutant."
Van Dommelen A., Keijers V., Somers E., Vanderleyden J.
Mol. Gen. Genet. 266:813-820(2002)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF149716 Genomic DNA. Translation: AAL87737.1.

3D structure databases

SMRQ8RQD1. Positions 76-358, 401-648.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.7.59. 1315.

Family and domain databases

HAMAPMF_00277. PII_uridylyl-transf.
[Tree]
InterProIPR002912. 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]
PANTHERPTHR13734:SF1. GlnD_Uridyltrans. 1 hit.
PfamPF01842. ACT. 2 hits.
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_AZOBR
AccessionPrimary (citable) accession number: Q8RQD1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2002
Last modified: February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents