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Protein

Rubredoxin-oxygen oxidoreductase

Gene

roo

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

Functioni

Catalyzes the four-electron reduction of one oxygen molecule to two water molecules.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: electron transfer

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi79Iron 11
Metal bindingi81Iron 11
Metal bindingi83Iron 21
Metal bindingi146Iron 11
Metal bindingi165Iron 11
Metal bindingi165Iron 21
Metal bindingi226Iron 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00092.

Names & Taxonomyi

Protein namesi
Recommended name:
Rubredoxin-oxygen oxidoreductase (EC:1.-.-.-)
Short name:
ROO
Short name:
Rubredoxin oxidase
Gene namesi
Name:roo
OrganismiDesulfovibrio gigas
Taxonomic identifieri879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002167921 – 402Rubredoxin-oxygen oxidoreductaseAdd BLAST402

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 17Combined sources8
Turni24 – 26Combined sources3
Beta strandi33 – 40Combined sources8
Beta strandi42 – 44Combined sources3
Beta strandi46 – 48Combined sources3
Helixi53 – 55Combined sources3
Helixi56 – 64Combined sources9
Helixi69 – 71Combined sources3
Beta strandi74 – 77Combined sources4
Helixi82 – 85Combined sources4
Helixi88 – 95Combined sources8
Beta strandi98 – 103Combined sources6
Helixi104 – 114Combined sources11
Beta strandi121 – 124Combined sources4
Beta strandi129 – 131Combined sources3
Beta strandi136 – 141Combined sources6
Beta strandi145 – 147Combined sources3
Beta strandi151 – 155Combined sources5
Turni156 – 159Combined sources4
Beta strandi160 – 164Combined sources5
Turni165 – 167Combined sources3
Helixi178 – 180Combined sources3
Helixi183 – 197Combined sources15
Helixi199 – 201Combined sources3
Helixi202 – 214Combined sources13
Beta strandi220 – 227Combined sources8
Beta strandi229 – 232Combined sources4
Helixi233 – 248Combined sources16
Beta strandi253 – 259Combined sources7
Beta strandi262 – 264Combined sources3
Helixi265 – 279Combined sources15
Beta strandi283 – 288Combined sources6
Turni289 – 291Combined sources3
Helixi294 – 302Combined sources9
Beta strandi305 – 310Combined sources6
Helixi320 – 331Combined sources12
Beta strandi338 – 348Combined sources11
Helixi350 – 361Combined sources12
Beta strandi371 – 376Combined sources6
Helixi379 – 400Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5DX-ray2.50A/B1-402[»]
ProteinModelPortaliQ9F0J6.
SMRiQ9F0J6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F0J6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini255 – 393Flavodoxin-likePROSITE-ProRule annotationAdd BLAST139

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 216Zinc metallo-hydrolaseAdd BLAST187

Sequence similaritiesi

In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family.Curated
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR001279. Metallo-B-lactamas.
IPR016440. Rubredoxin-O_OxRdtase.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005243. ROO. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56281. SSF56281. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9F0J6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQATKIIDGF HLVGAIDWNS RDFHGYTLSP MGTTYNAYLV EDEKTTLFDT
60 70 80 90 100
VKAEYKGELL CGIASVIDPK KIDYLVIQHL ELDHAGALPA LIEACQPEKI
110 120 130 140 150
FTSSLGQKAM ESHFHYKDWP VQVVKHGETL SLGKRTVTFY ETRMLHWPDS
160 170 180 190 200
MVSWFADEKV LISNDIFGQN IAASERFSDQ IPVHTLERAM REYYANIVNP
210 220 230 240 250
YAPQTLKAIE TLVGAGVAPE FICPDHGVIF RGADQCTFAV QKYVEYAEQK
260 270 280 290 300
PTNKVVIFYD SMWHSTEKMA RVLAESFRDE GCTVKLMWCK ACHHSQIMSE
310 320 330 340 350
ISDAGAVIVG SPTHNNGILP YVAGTLQYIK GLRPQNKIGG AFGSFGWSGE
360 370 380 390 400
STKVLAEWLT GMGFDMPATP VKVKNVPTHA DYEQLKTMAQ TIARALKAKL

AA
Length:402
Mass (Da):44,796
Last modified:March 1, 2001 - v1
Checksum:i50E8A87481A6B2D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218053 Genomic DNA. Translation: AAG34792.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218053 Genomic DNA. Translation: AAG34792.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5DX-ray2.50A/B1-402[»]
ProteinModelPortaliQ9F0J6.
SMRiQ9F0J6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00092.

Miscellaneous databases

EvolutionaryTraceiQ9F0J6.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR001279. Metallo-B-lactamas.
IPR016440. Rubredoxin-O_OxRdtase.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005243. ROO. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56281. SSF56281. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiROO_DESGI
AccessioniPrimary (citable) accession number: Q9F0J6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 76 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

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.