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Protein

ADP-ribosyl-[dinitrogen reductase] glycohydrolase

Gene

draG

Organism
Rhodospirillum rubrum
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHydrolase
Biological processNitrogen 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

Proteomic databases

PRIDEiP14300

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

Gene3Di1.10.4080.10, 1 hit
InterProiView protein in InterPro
IPR013479 ADP-ribosyl_diN_reduct_hydro
IPR005502 Ribosyl_crysJ1
IPR036705 Ribosyl_crysJ1_sf
PfamiView protein in Pfam
PF03747 ADP_ribosyl_GH, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiDRAG_RHORU
AccessioniPrimary (citable) accession number: P14300
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 23, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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