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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron 1
Metal bindingi81 – 811Iron 1
Metal bindingi83 – 831Iron 2
Metal bindingi146 – 1461Iron 1
Metal bindingi165 – 1651Iron 1
Metal bindingi165 – 1651Iron 2
Metal bindingi226 – 2261Iron 2

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402Rubredoxin-oxygen oxidoreductasePRO_0000216792Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
402
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 178Combined sources
Turni24 – 263Combined sources
Beta strandi33 – 408Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 483Combined sources
Helixi53 – 553Combined sources
Helixi56 – 649Combined sources
Helixi69 – 713Combined sources
Beta strandi74 – 774Combined sources
Helixi82 – 854Combined sources
Helixi88 – 958Combined sources
Beta strandi98 – 1036Combined sources
Helixi104 – 11411Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi136 – 1416Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi151 – 1555Combined sources
Turni156 – 1594Combined sources
Beta strandi160 – 1645Combined sources
Turni165 – 1673Combined sources
Helixi178 – 1803Combined sources
Helixi183 – 19715Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 21413Combined sources
Beta strandi220 – 2278Combined sources
Beta strandi229 – 2324Combined sources
Helixi233 – 24816Combined sources
Beta strandi253 – 2597Combined sources
Beta strandi262 – 2643Combined sources
Helixi265 – 27915Combined sources
Beta strandi283 – 2886Combined sources
Turni289 – 2913Combined sources
Helixi294 – 3029Combined sources
Beta strandi305 – 3106Combined sources
Helixi320 – 33112Combined sources
Beta strandi338 – 34811Combined sources
Helixi350 – 36112Combined sources
Beta strandi371 – 3766Combined sources
Helixi379 – 40022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5DX-ray2.50A/B1-402[»]
ProteinModelPortaliQ9F0J6.
SMRiQ9F0J6. Positions 2-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F0J6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 393139Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 216187Zinc metallo-hydrolaseAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5DX-ray2.50A/B1-402[»]
ProteinModelPortaliQ9F0J6.
SMRiQ9F0J6. Positions 2-392.
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...

Publicationsi

  1. "Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin."
    Gomes C.M., Silva G., Oliveira S., LeGall J., Liu M.-Y., Xavier A.V., Rodrigues-Pousada C., Teixeira M.
    J. Biol. Chem. 272:22502-22508(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  2. "Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the 'strict anaerobe' Desulfovibrio gigas."
    Chen L., Liu M.-Y., LeGall J., Fareleira P., Santos H., Xavier A.V.
    Biochem. Biophys. Res. Commun. 193:100-105(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, SUBUNIT.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.

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: January 20, 2016
This is version 74 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.