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Protein

Rubredoxin-2

Gene

alkG

Organism
Pseudomonas oleovorans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.2 Publications

Cofactori

Fe3+1 PublicationNote: Binds 2 Fe3+ ions per subunit.1 Publication

Pathwayi: alkane degradation

This protein is involved in the pathway alkane degradation, which is part of Hydrocarbon metabolism.
View all proteins of this organism that are known to be involved in the pathway alkane degradation and in Hydrocarbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi6 – 61Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi9 – 91Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi39 – 391Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi42 – 421Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi124 – 1241Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi127 – 1271Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi157 – 1571Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi160 – 1601Iron 2PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3844.
UniPathwayiUPA00191.

Names & Taxonomyi

Protein namesi
Recommended name:
Rubredoxin-2
Short name:
Rdxs
Alternative name(s):
Two-iron rubredoxin
Gene namesi
Name:alkG
Encoded oniPlasmid OCT0 Publication
OrganismiPseudomonas oleovorans
Taxonomic identifieri301 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas oleovorans/pseudoalcaligenes group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 173172Rubredoxin-2PRO_0000135044Add
BLAST

Expressioni

Inductioni

Induced by AlkS and n-alkanes.2 Publications

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi121 – 1244Combined sources
Turni125 – 1273Combined sources
Beta strandi130 – 1323Combined sources
Turni138 – 1414Combined sources
Helixi148 – 1503Combined sources
Beta strandi158 – 1603Combined sources
Helixi164 – 1663Combined sources
Beta strandi167 – 1693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S24NMR-A87-173[»]
ProteinModelPortaliP00272.
SMRiP00272. Positions 118-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00272.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 5352Rubredoxin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 17052Rubredoxin-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the rubredoxin family.Curated
Contains 2 rubredoxin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.20.28.10. 2 hits.
InterProiIPR024934. Rubredoxin-like_dom.
IPR004039. Rubredoxin-type_fold.
IPR024935. Rubredoxin_dom.
IPR018527. Rubredoxin_Fe_BS.
[Graphical view]
PfamiPF00301. Rubredoxin. 2 hits.
[Graphical view]
PRINTSiPR00163. RUBREDOXIN.
PROSITEiPS00202. RUBREDOXIN. 2 hits.
PS50903. RUBREDOXIN_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASYKCPDCN YVYDESAGNV HEGFSPGTPW HLIPEDWCCP DCAVRDKLDF
60 70 80 90 100
MLIESGVGEK GVTSTHTSPN LSEVSGTSLT AEAVVAPTSL EKLPSADVKG
110 120 130 140 150
QDLYKTQPPR SDAQGGKAYL KWICITCGHI YDEALGDEAE GFTPGTRFED
160 170
IPDDWCCPDC GATKEDYVLY EEK
Length:173
Mass (Da):18,899
Last modified:January 23, 2007 - v3
Checksum:i8CA9C654978FDF7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 414CCPD → DCPC AA sequence (PubMed:5543946).Curated
Sequence conflicti107 – 1071Q → E AA sequence (PubMed:5543946).Curated
Sequence conflicti114 – 1141Q → E AA sequence (PubMed:5543946).Curated
Sequence conflicti133 – 1331E → EW AA sequence (PubMed:5543946).Curated
Sequence conflicti154 – 1552DW → WD AA sequence (PubMed:5543946).Curated
Sequence conflicti158 – 1603PDC → WCBP AA sequence (PubMed:5543946).Curated
Sequence conflicti166 – 1661D → N AA sequence (PubMed:5543946).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245436 Genomic DNA. Translation: CAB54052.1.
PIRiB32850. RUPSEO.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245436 Genomic DNA. Translation: CAB54052.1.
PIRiB32850. RUPSEO.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S24NMR-A87-173[»]
ProteinModelPortaliP00272.
SMRiP00272. Positions 118-173.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00191.
BioCyciMetaCyc:MONOMER-3844.

Miscellaneous databases

EvolutionaryTraceiP00272.

Family and domain databases

Gene3Di2.20.28.10. 2 hits.
InterProiIPR024934. Rubredoxin-like_dom.
IPR004039. Rubredoxin-type_fold.
IPR024935. Rubredoxin_dom.
IPR018527. Rubredoxin_Fe_BS.
[Graphical view]
PfamiPF00301. Rubredoxin. 2 hits.
[Graphical view]
PRINTSiPR00163. RUBREDOXIN.
PROSITEiPS00202. RUBREDOXIN. 2 hits.
PS50903. RUBREDOXIN_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase."
    Kok M., Oldenhuis R., van der Linden M.P.G., Meulenberg C.H.C., Kingma J., Witholt B.
    J. Biol. Chem. 264:5442-5451(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: GPo1.
  2. "Evolutionary and phylogenetic relationships of rubredoxin-containing microbes."
    Benson A.M., Tomoda K., Chang J., Matsueda G., Lode E.T., Coon M.J., Yasunobu K.T.
    Biochem. Biophys. Res. Commun. 42:640-646(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-173.
  3. "Enzymatic omega-oxidation. 3. Purification and properties of rubredoxin, a component of the omega-hydroxylation system of Pseudomonas oleovorans."
    Peterson J.A., Coon M.J.
    J. Biol. Chem. 243:329-334(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  4. "Electron transfer from flavin to iron in the Pseudomonas oleovorans rubredoxin reductase-rubredoxin electron transfer complex."
    Lee H.J., Basran J., Scrutton N.S.
    Biochemistry 37:15513-15522(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON TRANSFER.
  5. "A positive feedback mechanism controls expression of AlkS, the transcriptional regulator of the Pseudomonas oleovorans alkane degradation pathway."
    Canosa I., Sanchez-Romero J.M., Yuste L., Rojo F.
    Mol. Microbiol. 35:791-799(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and characterization of the individual iron-binding domains by optical, CD and NMR spectroscopies."
    Perry A., Lian L.-Y., Scrutton N.S.
    Biochem. J. 354:89-98(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Differential expression of the components of the two alkane hydroxylases from Pseudomonas aeruginosa."
    Marin M.M., Yuste L., Rojo F.
    J. Bacteriol. 185:3232-3237(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase."
    Perry A., Tambyrajah W., Grossmann J.G., Lian L.Y., Scrutton N.S.
    Biochemistry 43:3167-3182(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 87-172 IN COMPLEX WITH IRON.

Entry informationi

Entry nameiRUBR2_PSEOL
AccessioniPrimary (citable) accession number: P00272
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Unlike other rubredoxins, this rubredoxin is unique in that it contains two binding sites for iron. It is most probably the product of a gene duplication event. The 2Fe form of the rubredoxin is a physiological form but it is less stable than the readily isolated 1Fe form. Both domains can form productive electron transfer complexes with rubredoxin reductase and accept electrons from the enzyme bound FAD.

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.