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Protein

Coenzyme A disulfide reductase

Gene

PH0572

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a coenzyme A disulfide reductase. Specific for CoA disulfide. Shows a slow NAD(P)H oxidase activity in the presence of high concentrations of substrate-level FAD. This demonstrates that it is not likely to act as an NADH oxidase in vivo.

Catalytic activityi

2 CoA + NADP+ = CoA-disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Kineticsi

KM value for NADH is lower than 9 µM.

  1. KM=73 µM for NADH

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius. Thermostable.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201SubstrateBy similarity
    Binding sitei24 – 241SubstrateBy similarity
    Binding sitei27 – 271SubstrateBy similarity
    Binding sitei44 – 441SubstrateBy similarity
    Active sitei48 – 481NucleophileBy similarity
    Active sitei48 – 481Redox-activeBy similarity
    Binding sitei75 – 751SubstrateBy similarity
    Binding sitei425 – 4251FAD; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 3826FADBy similarityAdd
    BLAST
    Nucleotide bindingi154 – 16916NADPBy similarityAdd
    BLAST
    Nucleotide bindingi273 – 28311FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-566-MONOMER.
    BRENDAi1.8.1.14. 5244.
    SABIO-RKO58308.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coenzyme A disulfide reductase (EC:1.8.1.14)
    Short name:
    CoA-disulfide reductase
    Short name:
    CoADR
    Gene namesi
    Ordered Locus Names:PH0572
    OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
    Taxonomic identifieri70601 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000000752 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Coenzyme A disulfide reductasePRO_0000184699Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi70601.PH0572.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125Combined sources
    Helixi16 – 2813Combined sources
    Beta strandi32 – 376Combined sources
    Beta strandi39 – 413Combined sources
    Beta strandi43 – 453Combined sources
    Helixi47 – 493Combined sources
    Helixi50 – 545Combined sources
    Helixi60 – 634Combined sources
    Beta strandi64 – 663Combined sources
    Helixi68 – 725Combined sources
    Turni73 – 753Combined sources
    Beta strandi78 – 803Combined sources
    Beta strandi84 – 896Combined sources
    Beta strandi92 – 965Combined sources
    Beta strandi103 – 1053Combined sources
    Beta strandi107 – 1115Combined sources
    Beta strandi115 – 1173Combined sources
    Turni124 – 1263Combined sources
    Helixi136 – 14813Combined sources
    Beta strandi153 – 1575Combined sources
    Helixi161 – 17111Combined sources
    Turni172 – 1743Combined sources
    Beta strandi176 – 1805Combined sources
    Beta strandi182 – 1854Combined sources
    Turni186 – 1905Combined sources
    Helixi193 – 20614Combined sources
    Beta strandi207 – 2104Combined sources
    Beta strandi215 – 23117Combined sources
    Beta strandi233 – 2353Combined sources
    Beta strandi237 – 2415Combined sources
    Beta strandi245 – 2473Combined sources
    Helixi250 – 2534Combined sources
    Turni254 – 2563Combined sources
    Beta strandi263 – 2664Combined sources
    Beta strandi278 – 2803Combined sources
    Helixi282 – 2843Combined sources
    Beta strandi285 – 2895Combined sources
    Turni290 – 2923Combined sources
    Beta strandi294 – 2963Combined sources
    Helixi301 – 31515Combined sources
    Beta strandi329 – 3335Combined sources
    Beta strandi336 – 3427Combined sources
    Helixi345 – 3506Combined sources
    Beta strandi355 – 36511Combined sources
    Beta strandi367 – 3704Combined sources
    Beta strandi374 – 3829Combined sources
    Turni383 – 3853Combined sources
    Beta strandi387 – 39711Combined sources
    Helixi399 – 41113Combined sources
    Helixi415 – 4195Combined sources
    Turni427 – 4293Combined sources
    Helixi435 – 4439Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KD9X-ray2.75A/B/C7-444[»]
    4FX9X-ray2.70A/B1-445[»]
    ProteinModelPortaliO58308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO58308.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiarCOG01069. Archaea.
    COG0446. LUCA.
    HOGENOMiHOG000276710.
    KOiK18367.
    OMAiFMPEYEP.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 2 hits.
    InterProiIPR017758. CoA_disulphide_reductase.
    IPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR03385. CoA_CoA_reduc. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O58308-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGENMKKKVV IIGGGAAGMS AASRVKRLKP EWDVKVFEAT EWVSHAPCGI
    60 70 80 90 100
    PYVVEGLSTP DKLMYYPPEV FIKKRGIDLH LNAEVIEVDT GYVRVRENGG
    110 120 130 140 150
    EKSYEWDYLV FANGASPQVP AIEGVNLKGV FTADLPPDAL AIREYMEKYK
    160 170 180 190 200
    VENVVIIGGG YIGIEMAEAF AAQGKNVTMI VRGERVLRRS FDKEVTDILE
    210 220 230 240 250
    EKLKKHVNLR LQEITMKIEG EERVEKVVTD AGEYKAELVI LATGIKPNIE
    260 270 280 290 300
    LAKQLGVRIG ETGAIWTNEK MQTSVENVYA AGDVAETRHV ITGRRVWVPL
    310 320 330 340 350
    APAGNKMGYV AGSNIAGKEL HFPGVLGTAV TKFMDVEIGK TGLTEMEALK
    360 370 380 390 400
    EGYDVRTAFI KASTRPHYYP GGREIWLKGV VDNETNRLLG VQVVGSDILP
    410 420 430 440
    RIDTAAAMLM AGFTTKDAFF TDLAYAPPFA PVWDPLIVLA RVLKF
    Length:445
    Mass (Da):48,977
    Last modified:August 1, 1998 - v1
    Checksum:i896A034000A0B233
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA. Translation: BAA29661.1.
    PIRiH71171.

    Genome annotation databases

    EnsemblBacteriaiBAA29661; BAA29661; BAA29661.
    KEGGipho:PH0572.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA. Translation: BAA29661.1.
    PIRiH71171.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KD9X-ray2.75A/B/C7-444[»]
    4FX9X-ray2.70A/B1-445[»]
    ProteinModelPortaliO58308.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi70601.PH0572.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA29661; BAA29661; BAA29661.
    KEGGipho:PH0572.

    Phylogenomic databases

    eggNOGiarCOG01069. Archaea.
    COG0446. LUCA.
    HOGENOMiHOG000276710.
    KOiK18367.
    OMAiFMPEYEP.

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-566-MONOMER.
    BRENDAi1.8.1.14. 5244.
    SABIO-RKO58308.

    Miscellaneous databases

    EvolutionaryTraceiO58308.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 2 hits.
    InterProiIPR017758. CoA_disulphide_reductase.
    IPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR03385. CoA_CoA_reduc. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCDR_PYRHO
    AccessioniPrimary (citable) accession number: O58308
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: August 1, 1998
    Last modified: September 7, 2016
    This is version 109 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, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.