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Protein

Reverse rubrerythrin-2

Gene

rbr3B

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as the terminal component of an NADH peroxidase (NADH:H2O2 oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) as the electron transport intermediary from NADH to revRbr 2. Plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Also exhibits NADH oxidase (NADH:O2 oxidoreductase) activity in vitro, which is 100-fold lesser than that of FprA1/2 using the same electron transfer components. Therefore, its predominant function is most likely as a scavenger of its preferred substrate, H2O2.1 Publication

Miscellaneous

This protein has been named "reverse" rubrerythrin (revRbr) because the order of the two functional domains is reversed compared to "classical" rubrerythrins: the rubredoxin-like FeS4 domain is located at the N-terminus and the ferritin-like diiron domain at the C-terminus.
A revRbr-overexpressing strain of C.acetobutylicum shows greatly increased tolerance to H2O2 and O2 exposure.

Catalytic activityi

NADH + H2O2 = NAD+ + 2 H2O.1 Publication

Cofactori

Fe3+1 PublicationNote: Binds 3 Fe3+ ions per subunit.1 Publication

Enzyme regulationi

Rubredoxin (Rd) increases the NADH consumption rate by serving as an intermediary electron-transfer shuttle between NROR and revRbr.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi6Iron 1By similarity1
Metal bindingi9Iron 1By similarity1
Metal bindingi22Iron 1By similarity1
Metal bindingi25Iron 1By similarity1
Metal bindingi69Iron 2By similarity1
Metal bindingi102Iron 2By similarity1
Metal bindingi102Iron 3By similarity1
Metal bindingi132Iron 3By similarity1
Metal bindingi165Iron 2By similarity1
Metal bindingi165Iron 3By similarity1
Metal bindingi168Iron 3By similarity1

GO - Molecular functioni

  • electron carrier activity Source: UniProtKB
  • iron ion binding Source: UniProtKB
  • NADH peroxidase activity Source: UniProtKB

GO - Biological processi

  • cellular response to alkaline pH Source: UniProtKB
  • cellular response to cold Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to oxygen levels Source: UniProtKB
  • cellular response to salt stress Source: UniProtKB
  • hydrogen peroxide catabolic process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processDetoxification, Electron transport, Stress response, Transport
LigandIron, Metal-binding, NAD

Enzyme and pathway databases

BRENDAi1.11.1.1. 1452.

Names & Taxonomyi

Protein namesi
Recommended name:
Reverse rubrerythrin-2
Short name:
revRbr 2
Alternative name(s):
NADH peroxidase (EC:1.11.1.1)
Short name:
NPXase
Short name:
Npx
Rubperoxin 2
Short name:
Rpr 2
Gene namesi
Name:rbr3B
Synonyms:hsp21, rpr2
Ordered Locus Names:CA_C3597
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004055351 – 181Reverse rubrerythrin-2Add BLAST181

Expressioni

Inductioni

Up-regulated by heat and oxidative stress (exposure to air, O2 and H2O2) (at mRNA and protein levels). Various other environmental stress conditions such as an increase of the pH of the growth medium from 4.5 to 6.2, addition of the salt NaCl or of the solvent butanol, and lowering the incubation temperature also result in transiently increased transcript levels. Is also expressed under non-stressful conditions. Repressed by PerR.5 Publications

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi272562.CA_C3597.

Structurei

3D structure databases

ProteinModelPortaliQ97D83.
SMRiQ97D83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 35Rubredoxin-likePROSITE-ProRule annotationAdd BLAST35
Domaini52 – 181Ferritin-like diironPROSITE-ProRule annotationAdd BLAST130

Phylogenomic databases

eggNOGiENOG4105KY8. Bacteria.
COG1592. LUCA.
HOGENOMiHOG000153104.
OMAiEKNWADE.

Family and domain databases

Gene3Di1.20.1260.10. 2 hits.
InterProiView protein in InterPro
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR024934. Rubredoxin-like_dom.
IPR003251. Rubrerythrin.
PfamiView protein in Pfam
PF02915. Rubrerythrin. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiView protein in PROSITE
PS50905. FERRITIN_LIKE. 1 hit.
PS50903. RUBREDOXIN_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q97D83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFKCVVCG YIYTGEDAPE KCPVCGAGKD KFVEVKDEGE GWADEHKIGI
60 70 80 90 100
AKGVDKEVLE GLRANFTGEC TEVGMYLAMA RQADREGYPE VAEAYKRIAF
110 120 130 140 150
EEAEHASKFA ELLGEVVVAD TKTNLQMRVD AEKGACEGKK ELATLAKKLN
160 170 180
YDAIHDTVHE MCKDEARHGS AFRGLLNRYF K
Length:181
Mass (Da):20,107
Last modified:October 1, 2001 - v1
Checksum:i181DCC858E7F8C93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK81520.1.
PIRiE97341.
RefSeqiNP_350180.1. NC_003030.1.
WP_010966860.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK81520; AAK81520; CA_C3597.
GeneIDi1119779.
KEGGicac:CA_C3597.
PATRICifig|272562.8.peg.3786.

Similar proteinsi

Entry informationi

Entry nameiRRBR2_CLOAB
AccessioniPrimary (citable) accession number: Q97D83
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: October 1, 2001
Last modified: June 7, 2017
This is version 96 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

Complete proteome, Direct protein sequencing, Reference proteome