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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)DescriptionActionsGraphical viewLength
    Binding sitei20SubstrateBy similarity1
    Binding sitei24SubstrateBy similarity1
    Binding sitei27SubstrateBy similarity1
    Binding sitei44SubstrateBy similarity1
    Active sitei48NucleophileBy similarity1
    Active sitei48Redox-activeBy similarity1
    Binding sitei75SubstrateBy similarity1
    Binding sitei425FAD; via carbonyl oxygenBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi13 – 38FADBy similarityAdd BLAST26
    Nucleotide bindingi154 – 169NADPBy similarityAdd BLAST16
    Nucleotide bindingi273 – 283FADBy similarityAdd BLAST11

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00001846991 – 445Coenzyme A disulfide reductaseAdd BLAST445

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi70601.PH0572.

    Structurei

    Secondary structure

    1445
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 12Combined sources5
    Helixi16 – 28Combined sources13
    Beta strandi32 – 37Combined sources6
    Beta strandi39 – 41Combined sources3
    Beta strandi43 – 45Combined sources3
    Helixi47 – 49Combined sources3
    Helixi50 – 54Combined sources5
    Helixi60 – 63Combined sources4
    Beta strandi64 – 66Combined sources3
    Helixi68 – 72Combined sources5
    Turni73 – 75Combined sources3
    Beta strandi78 – 80Combined sources3
    Beta strandi84 – 89Combined sources6
    Beta strandi92 – 96Combined sources5
    Beta strandi103 – 105Combined sources3
    Beta strandi107 – 111Combined sources5
    Beta strandi115 – 117Combined sources3
    Turni124 – 126Combined sources3
    Helixi136 – 148Combined sources13
    Beta strandi153 – 157Combined sources5
    Helixi161 – 171Combined sources11
    Turni172 – 174Combined sources3
    Beta strandi176 – 180Combined sources5
    Beta strandi182 – 185Combined sources4
    Turni186 – 190Combined sources5
    Helixi193 – 206Combined sources14
    Beta strandi207 – 210Combined sources4
    Beta strandi215 – 231Combined sources17
    Beta strandi233 – 235Combined sources3
    Beta strandi237 – 241Combined sources5
    Beta strandi245 – 247Combined sources3
    Helixi250 – 253Combined sources4
    Turni254 – 256Combined sources3
    Beta strandi263 – 266Combined sources4
    Beta strandi278 – 280Combined sources3
    Helixi282 – 284Combined sources3
    Beta strandi285 – 289Combined sources5
    Turni290 – 292Combined sources3
    Beta strandi294 – 296Combined sources3
    Helixi301 – 315Combined sources15
    Beta strandi329 – 333Combined sources5
    Beta strandi336 – 342Combined sources7
    Helixi345 – 350Combined sources6
    Beta strandi355 – 365Combined sources11
    Beta strandi367 – 370Combined sources4
    Beta strandi374 – 382Combined sources9
    Turni383 – 385Combined sources3
    Beta strandi387 – 397Combined sources11
    Helixi399 – 411Combined sources13
    Helixi415 – 419Combined sources5
    Turni427 – 429Combined sources3
    Helixi435 – 443Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3KD9X-ray2.75A/B/C7-444[»]
    4FX9X-ray2.70A/B1-445[»]
    ProteinModelPortaliO58308.
    SMRiO58308.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3KD9X-ray2.75A/B/C7-444[»]
    4FX9X-ray2.70A/B1-445[»]
    ProteinModelPortaliO58308.
    SMRiO58308.
    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: November 2, 2016
    This is version 110 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.