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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)DescriptionActionsGraphical viewLength
Metal bindingi6Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi9Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi39Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi42Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi124Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi127Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi157Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi160Iron 2PROSITE-ProRule annotation1 Publication1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001350442 – 173Rubredoxin-2Add BLAST172

Expressioni

Inductioni

Induced by AlkS and n-alkanes.2 Publications

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi121 – 124Combined sources4
Turni125 – 127Combined sources3
Beta strandi130 – 132Combined sources3
Turni138 – 141Combined sources4
Helixi148 – 150Combined sources3
Beta strandi158 – 160Combined sources3
Helixi164 – 166Combined sources3
Beta strandi167 – 169Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00272.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 53Rubredoxin-like 1PROSITE-ProRule annotationAdd BLAST52
Domaini119 – 170Rubredoxin-like 2PROSITE-ProRule annotationAdd BLAST52

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00730. rubredoxin. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti38 – 41CCPD → DCPC AA sequence (PubMed:5543946).Curated4
Sequence conflicti107Q → E AA sequence (PubMed:5543946).Curated1
Sequence conflicti114Q → E AA sequence (PubMed:5543946).Curated1
Sequence conflicti133E → EW AA sequence (PubMed:5543946).Curated1
Sequence conflicti154 – 155DW → WD AA sequence (PubMed:5543946).Curated2
Sequence conflicti158 – 160PDC → WCBP AA sequence (PubMed:5543946).Curated3
Sequence conflicti166D → N AA sequence (PubMed:5543946).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S24NMR-A87-173[»]
ProteinModelPortaliP00272.
SMRiP00272.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00191.
BioCyciMetaCyc:MONOMER-3844.

Miscellaneous databases

EvolutionaryTraceiP00272.

Family and domain databases

CDDicd00730. rubredoxin. 2 hits.
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...

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: November 2, 2016
This is version 120 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.