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Protein

ADP-ribosyl-[dinitrogen reductase] glycohydrolase

Gene

draG

Organism
Rhodospirillum rubrum
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the regulation of the nitrogen fixation activity by the reversible ADP-ribosylation of the dinitrogenase reductase component of the nitrogenase enzyme complex. The ADP-ribosyltransferase (DraT) transfers the ADP-ribose group from NAD to dinitrogenase reductase. The ADP-ribose group is removed through the action of the ADP-ribosylglycohydrolase (DraG).

Catalytic activityi

[Dinitrogen reductase]-N(omega)-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine.

GO - Molecular functioni

GO - Biological processi

  • nitrogen fixation Source: UniProtKB-KW
  • protein de-ADP-ribosylation Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nitrogen fixation

Enzyme and pathway databases

BRENDAi3.2.2.24. 5420.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosyl-[dinitrogen reductase] glycohydrolase (EC:3.2.2.24)
Short name:
ADP-ribosylglycohydrolase
Alternative name(s):
Dinitrogenase reductase-activating glycohydrolase
Gene namesi
Name:draG
OrganismiRhodospirillum rubrum
Taxonomic identifieri1085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001572861 – 294ADP-ribosyl-[dinitrogen reductase] glycohydrolaseAdd BLAST294

Interactioni

Protein-protein interaction databases

STRINGi269796.Rru_A1008.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 25Combined sources20
Turni26 – 29Combined sources4
Helixi32 – 39Combined sources8
Turni49 – 52Combined sources4
Helixi60 – 75Combined sources16
Helixi80 – 92Combined sources13
Helixi100 – 112Combined sources13
Helixi129 – 131Combined sources3
Helixi133 – 138Combined sources6
Turni139 – 141Combined sources3
Helixi143 – 145Combined sources3
Helixi146 – 154Combined sources9
Turni155 – 157Combined sources3
Helixi161 – 178Combined sources18
Helixi182 – 196Combined sources15
Helixi198 – 200Combined sources3
Beta strandi210 – 212Combined sources3
Helixi213 – 225Combined sources13
Helixi230 – 239Combined sources10
Beta strandi241 – 243Combined sources3
Helixi244 – 259Combined sources16
Helixi261 – 263Combined sources3
Helixi266 – 269Combined sources4
Helixi274 – 291Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WOCX-ray2.20A/B/C1-294[»]
2WODX-ray2.25A/B1-294[»]
2WOEX-ray1.90A/B/C1-294[»]
ProteinModelPortaliP14300.
SMRiP14300.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14300.

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosylglycohydrolase family.Curated

Phylogenomic databases

eggNOGiENOG41065RQ. Bacteria.
COG1397. LUCA.

Family and domain databases

InterProiIPR013479. ADP-ribosyl_diN_reduct_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMiSSF101478. SSF101478. 1 hit.
TIGRFAMsiTIGR02662. dinitro_DRAG. 1 hit.

Sequencei

Sequence statusi: Complete.

P14300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGPSVHDRA LGAFLGLAVG DALGATVEFM TKGEIAQQYG IHRKMTGGGW
60 70 80 90 100
LRLKPGQITD DTEMSLALGR SLAAKGTLDV ADICEEFALW LKSRPVDVGN
110 120 130 140 150
TCRRGIRRYM HEGTTTAPYS EGDAGNGAAM RCLPAALATL GHPADLEPWV
160 170 180 190 200
LAQARITHNH PLSDAACLTL GRMVHHLIGG RGMKACREEA NRLVHQHRDF
210 220 230 240 250
HFEPYKGQSS AYIVDTMQTV LHYYFVTDTF KSCLIQTVNQ GGDADTTGAL
260 270 280 290
AGMLAGATYG VDDIPSGWLS KLDMKVEREI RRQVDALLAL AGLD
Length:294
Mass (Da):31,792
Last modified:January 1, 1990 - v1
Checksum:i5E72ECFA8A798368
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16187 Genomic DNA. Translation: CAA34310.1.
PIRiJT0536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16187 Genomic DNA. Translation: CAA34310.1.
PIRiJT0536.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WOCX-ray2.20A/B/C1-294[»]
2WODX-ray2.25A/B1-294[»]
2WOEX-ray1.90A/B/C1-294[»]
ProteinModelPortaliP14300.
SMRiP14300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269796.Rru_A1008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG41065RQ. Bacteria.
COG1397. LUCA.

Enzyme and pathway databases

BRENDAi3.2.2.24. 5420.

Miscellaneous databases

EvolutionaryTraceiP14300.

Family and domain databases

InterProiIPR013479. ADP-ribosyl_diN_reduct_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMiSSF101478. SSF101478. 1 hit.
TIGRFAMsiTIGR02662. dinitro_DRAG. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDRAG_RHORU
AccessioniPrimary (citable) accession number: P14300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.