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P00183

- CPXA_PSEPU

UniProt

P00183 - CPXA_PSEPU

Protein

Camphor 5-monooxygenase

Gene

camC

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in a camphor oxidation system.

    Catalytic activityi

    +-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O.

    Cofactori

    Heme group.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi358 – 3581Iron (heme axial ligand)

    GO - Molecular functioni

    1. camphor 5-monooxygenase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. (+)-camphor catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3021.
    UniPathwayiUPA00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Camphor 5-monooxygenase (EC:1.14.15.1)
    Alternative name(s):
    Cytochrome P450-cam
    Short name:
    Cytochrome P450cam
    Gene namesi
    Name:camC
    Synonyms:cyp101
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 415414Camphor 5-monooxygenasePRO_0000052204Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-29809N.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 83
    Helixi21 – 233
    Beta strandi29 – 313
    Helixi35 – 373
    Helixi39 – 435
    Helixi44 – 474
    Beta strandi48 – 514
    Beta strandi53 – 575
    Helixi59 – 613
    Beta strandi63 – 664
    Helixi69 – 779
    Turni79 – 813
    Beta strandi82 – 865
    Beta strandi88 – 903
    Helixi91 – 966
    Turni100 – 1034
    Turni106 – 1083
    Helixi109 – 12012
    Helixi122 – 14322
    Helixi144 – 1463
    Beta strandi147 – 1504
    Helixi151 – 1544
    Turni155 – 1573
    Helixi158 – 16811
    Helixi172 – 1743
    Helixi175 – 18612
    Beta strandi190 – 1923
    Helixi194 – 21421
    Helixi220 – 2256
    Beta strandi230 – 2334
    Helixi236 – 25116
    Helixi253 – 26614
    Helixi269 – 2779
    Helixi279 – 2813
    Helixi282 – 29211
    Beta strandi298 – 3047
    Beta strandi306 – 3083
    Beta strandi311 – 3133
    Beta strandi318 – 3214
    Helixi323 – 3286
    Turni330 – 3323
    Beta strandi333 – 3353
    Helixi354 – 3563
    Helixi361 – 37818
    Beta strandi382 – 3843
    Beta strandi395 – 3973
    Beta strandi399 – 4013
    Beta strandi404 – 4063
    Helixi409 – 4113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AKDX-ray1.80A2-415[»]
    1C8JX-ray2.10A/B2-415[»]
    1CP4X-ray1.90A2-415[»]
    1DZ4X-ray1.60A/B2-415[»]
    1DZ6X-ray1.90A/B2-415[»]
    1DZ8X-ray1.90A/B2-415[»]
    1DZ9X-ray1.90A/B2-415[»]
    1GEBX-ray2.03A1-415[»]
    1GEKX-ray1.70A1-415[»]
    1GEMX-ray2.00A1-415[»]
    1GJMX-ray2.20A2-415[»]
    1IWIX-ray2.00A1-415[»]
    1IWJX-ray2.00A1-415[»]
    1IWKX-ray2.00A1-415[»]
    1J51X-ray2.20A/B/C/D2-415[»]
    1K2OX-ray1.65A/B2-415[»]
    1LWLX-ray2.20A1-415[»]
    1MPWX-ray2.34A/B2-415[»]
    1NOOX-ray2.20A2-415[»]
    1O76X-ray1.80A/B2-415[»]
    1P2YX-ray2.30A2-415[»]
    1P7RX-ray2.85A2-415[»]
    1PHAX-ray1.63A2-415[»]
    1PHBX-ray1.60A2-415[»]
    1PHCX-ray1.60A2-415[»]
    1PHDX-ray1.60A2-415[»]
    1PHEX-ray1.60A2-415[»]
    1PHFX-ray1.60A2-415[»]
    1PHGX-ray1.60A2-415[»]
    1QMQX-ray1.55A2-415[»]
    1RE9X-ray1.45A2-415[»]
    1RF9X-ray1.80A1-415[»]
    1T85X-ray1.80A2-415[»]
    1T86X-ray1.90A/B2-415[»]
    1T87X-ray1.80A/B2-415[»]
    1T88X-ray1.90A/B2-415[»]
    1UYUX-ray2.00A/B2-415[»]
    1YRCX-ray1.40A2-415[»]
    1YRDX-ray1.70A2-415[»]
    2A1MX-ray2.10A/B1-415[»]
    2A1NX-ray1.90A/B1-415[»]
    2A1OX-ray1.55A/B1-415[»]
    2CP4X-ray2.10A2-415[»]
    2CPPX-ray1.63A2-415[»]
    2FE6X-ray1.50A1-415[»]
    2FERX-ray1.70A11-415[»]
    2FEUX-ray1.70A/B11-415[»]
    2FRZX-ray2.10A/B2-415[»]
    2GQXX-ray2.10A/B11-415[»]
    2GR6X-ray2.30A/B11-415[»]
    2H7QX-ray1.50A2-415[»]
    2H7RX-ray2.10A2-415[»]
    2H7SX-ray2.15A/C2-415[»]
    2L8MNMR-A1-415[»]
    2LQDNMR-A11-415[»]
    2M56NMR-A12-415[»]
    2QBLX-ray1.80A1-415[»]
    2QBMX-ray1.80A1-415[»]
    2QBNX-ray1.75A1-415[»]
    2QBOX-ray1.90A1-415[»]
    2Z97X-ray1.80A1-415[»]
    2ZAWX-ray1.55A1-415[»]
    2ZAXX-ray1.60A1-415[»]
    2ZUHX-ray1.55A1-415[»]
    2ZUIX-ray1.50A1-415[»]
    2ZUJX-ray1.60A1-415[»]
    2ZWTX-ray1.35A1-415[»]
    2ZWUX-ray1.30A1-415[»]
    3CP4X-ray2.30A2-415[»]
    3CPPX-ray1.90A2-415[»]
    3FWFX-ray1.83A/B11-415[»]
    3FWGX-ray1.55A/B11-415[»]
    3FWIX-ray2.40A11-415[»]
    3FWJX-ray1.90A11-415[»]
    3L61X-ray1.50A2-415[»]
    3L62X-ray1.70A2-415[»]
    3L63X-ray1.50A2-415[»]
    3OIAX-ray1.65A2-415[»]
    3OL5X-ray1.75A2-415[»]
    3P6MX-ray2.00A2-415[»]
    3P6NX-ray1.70A2-415[»]
    3P6OX-ray2.00A2-415[»]
    3P6PX-ray1.90A2-415[»]
    3P6QX-ray1.95A2-415[»]
    3P6RX-ray2.10A2-415[»]
    3P6SX-ray2.00A2-415[»]
    3P6TX-ray1.90A2-415[»]
    3P6UX-ray1.70A2-415[»]
    3P6VX-ray2.00A2-415[»]
    3P6WX-ray2.10A2-415[»]
    3P6XX-ray1.65A2-415[»]
    3W9CX-ray2.50A2-415[»]
    4CP4X-ray2.10A2-415[»]
    4CPPX-ray2.11A2-415[»]
    4EK1X-ray1.97A/B2-415[»]
    4G3RX-ray2.20A/B2-415[»]
    4JWSX-ray2.15A/B1-415[»]
    4JWUX-ray2.20A/B1-415[»]
    4JX1X-ray2.09A/B/E/F1-415[»]
    4KKYX-ray2.00X2-414[»]
    4L49X-ray2.13A1-415[»]
    4L4AX-ray2.10A1-415[»]
    4L4BX-ray2.10A1-415[»]
    4L4CX-ray2.20A/B1-415[»]
    4L4DX-ray2.10A1-415[»]
    4L4EX-ray1.26A1-415[»]
    4L4FX-ray1.29A1-415[»]
    4L4GX-ray1.55A1-415[»]
    5CP4X-ray1.75A2-415[»]
    5CPPX-ray2.08A2-415[»]
    6CP4X-ray1.90A2-415[»]
    6CPPX-ray1.90A2-415[»]
    7CPPX-ray2.00A2-415[»]
    8CPPX-ray2.10A2-415[»]
    ProteinModelPortaliP00183.
    SMRiP00183. Positions 10-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00183.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00183-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTETIQSNA NLAPLPPHVP EHLVFDFDMY NPSNLSAGVQ EAWAVLQESN    50
    VPDLVWTRCN GGHWIATRGQ LIREAYEDYR HFSSECPFIP REAGEAYDFI 100
    PTSMDPPEQR QFRALANQVV GMPVVDKLEN RIQELACSLI ESLRPQGQCN 150
    FTEDYAEPFP IRIFMLLAGL PEEDIPHLKY LTDQMTRPDG SMTFAEAKEA 200
    LYDYLIPIIE QRRQKPGTDA ISIVANGQVN GRPITSDEAK RMCGLLLVGG 250
    LDTVVNFLSF SMEFLAKSPE HRQELIERPE RIPAACEELL RRFSLVADGR 300
    ILTSDYEFHG VQLKKGDQIL LPQMLSGLDE RENACPMHVD FSRQKVSHTT 350
    FGHGSHLCLG QHLARREIIV TLKEWLTRIP DFSIAPGAQI QHKSGIVSGV 400
    QALPLVWDPA TTKAV 415
    Length:415
    Mass (Da):46,669
    Last modified:January 23, 2007 - v2
    Checksum:iE84641B4A65DD2D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 572Missing AA sequence (PubMed:7130171)Curated
    Sequence conflicti277 – 2771E → Q AA sequence (PubMed:7130171)Curated
    Sequence conflicti362 – 3621H → S AA sequence (PubMed:7130171)Curated
    Sequence conflicti408 – 4081D → N AA sequence (PubMed:7130171)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12546 Genomic DNA. Translation: AAA25760.1.
    D00528 Genomic DNA. Translation: BAA00412.1.
    PIRiA25660. O4PSCP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12546 Genomic DNA. Translation: AAA25760.1 .
    D00528 Genomic DNA. Translation: BAA00412.1 .
    PIRi A25660. O4PSCP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AKD X-ray 1.80 A 2-415 [» ]
    1C8J X-ray 2.10 A/B 2-415 [» ]
    1CP4 X-ray 1.90 A 2-415 [» ]
    1DZ4 X-ray 1.60 A/B 2-415 [» ]
    1DZ6 X-ray 1.90 A/B 2-415 [» ]
    1DZ8 X-ray 1.90 A/B 2-415 [» ]
    1DZ9 X-ray 1.90 A/B 2-415 [» ]
    1GEB X-ray 2.03 A 1-415 [» ]
    1GEK X-ray 1.70 A 1-415 [» ]
    1GEM X-ray 2.00 A 1-415 [» ]
    1GJM X-ray 2.20 A 2-415 [» ]
    1IWI X-ray 2.00 A 1-415 [» ]
    1IWJ X-ray 2.00 A 1-415 [» ]
    1IWK X-ray 2.00 A 1-415 [» ]
    1J51 X-ray 2.20 A/B/C/D 2-415 [» ]
    1K2O X-ray 1.65 A/B 2-415 [» ]
    1LWL X-ray 2.20 A 1-415 [» ]
    1MPW X-ray 2.34 A/B 2-415 [» ]
    1NOO X-ray 2.20 A 2-415 [» ]
    1O76 X-ray 1.80 A/B 2-415 [» ]
    1P2Y X-ray 2.30 A 2-415 [» ]
    1P7R X-ray 2.85 A 2-415 [» ]
    1PHA X-ray 1.63 A 2-415 [» ]
    1PHB X-ray 1.60 A 2-415 [» ]
    1PHC X-ray 1.60 A 2-415 [» ]
    1PHD X-ray 1.60 A 2-415 [» ]
    1PHE X-ray 1.60 A 2-415 [» ]
    1PHF X-ray 1.60 A 2-415 [» ]
    1PHG X-ray 1.60 A 2-415 [» ]
    1QMQ X-ray 1.55 A 2-415 [» ]
    1RE9 X-ray 1.45 A 2-415 [» ]
    1RF9 X-ray 1.80 A 1-415 [» ]
    1T85 X-ray 1.80 A 2-415 [» ]
    1T86 X-ray 1.90 A/B 2-415 [» ]
    1T87 X-ray 1.80 A/B 2-415 [» ]
    1T88 X-ray 1.90 A/B 2-415 [» ]
    1UYU X-ray 2.00 A/B 2-415 [» ]
    1YRC X-ray 1.40 A 2-415 [» ]
    1YRD X-ray 1.70 A 2-415 [» ]
    2A1M X-ray 2.10 A/B 1-415 [» ]
    2A1N X-ray 1.90 A/B 1-415 [» ]
    2A1O X-ray 1.55 A/B 1-415 [» ]
    2CP4 X-ray 2.10 A 2-415 [» ]
    2CPP X-ray 1.63 A 2-415 [» ]
    2FE6 X-ray 1.50 A 1-415 [» ]
    2FER X-ray 1.70 A 11-415 [» ]
    2FEU X-ray 1.70 A/B 11-415 [» ]
    2FRZ X-ray 2.10 A/B 2-415 [» ]
    2GQX X-ray 2.10 A/B 11-415 [» ]
    2GR6 X-ray 2.30 A/B 11-415 [» ]
    2H7Q X-ray 1.50 A 2-415 [» ]
    2H7R X-ray 2.10 A 2-415 [» ]
    2H7S X-ray 2.15 A/C 2-415 [» ]
    2L8M NMR - A 1-415 [» ]
    2LQD NMR - A 11-415 [» ]
    2M56 NMR - A 12-415 [» ]
    2QBL X-ray 1.80 A 1-415 [» ]
    2QBM X-ray 1.80 A 1-415 [» ]
    2QBN X-ray 1.75 A 1-415 [» ]
    2QBO X-ray 1.90 A 1-415 [» ]
    2Z97 X-ray 1.80 A 1-415 [» ]
    2ZAW X-ray 1.55 A 1-415 [» ]
    2ZAX X-ray 1.60 A 1-415 [» ]
    2ZUH X-ray 1.55 A 1-415 [» ]
    2ZUI X-ray 1.50 A 1-415 [» ]
    2ZUJ X-ray 1.60 A 1-415 [» ]
    2ZWT X-ray 1.35 A 1-415 [» ]
    2ZWU X-ray 1.30 A 1-415 [» ]
    3CP4 X-ray 2.30 A 2-415 [» ]
    3CPP X-ray 1.90 A 2-415 [» ]
    3FWF X-ray 1.83 A/B 11-415 [» ]
    3FWG X-ray 1.55 A/B 11-415 [» ]
    3FWI X-ray 2.40 A 11-415 [» ]
    3FWJ X-ray 1.90 A 11-415 [» ]
    3L61 X-ray 1.50 A 2-415 [» ]
    3L62 X-ray 1.70 A 2-415 [» ]
    3L63 X-ray 1.50 A 2-415 [» ]
    3OIA X-ray 1.65 A 2-415 [» ]
    3OL5 X-ray 1.75 A 2-415 [» ]
    3P6M X-ray 2.00 A 2-415 [» ]
    3P6N X-ray 1.70 A 2-415 [» ]
    3P6O X-ray 2.00 A 2-415 [» ]
    3P6P X-ray 1.90 A 2-415 [» ]
    3P6Q X-ray 1.95 A 2-415 [» ]
    3P6R X-ray 2.10 A 2-415 [» ]
    3P6S X-ray 2.00 A 2-415 [» ]
    3P6T X-ray 1.90 A 2-415 [» ]
    3P6U X-ray 1.70 A 2-415 [» ]
    3P6V X-ray 2.00 A 2-415 [» ]
    3P6W X-ray 2.10 A 2-415 [» ]
    3P6X X-ray 1.65 A 2-415 [» ]
    3W9C X-ray 2.50 A 2-415 [» ]
    4CP4 X-ray 2.10 A 2-415 [» ]
    4CPP X-ray 2.11 A 2-415 [» ]
    4EK1 X-ray 1.97 A/B 2-415 [» ]
    4G3R X-ray 2.20 A/B 2-415 [» ]
    4JWS X-ray 2.15 A/B 1-415 [» ]
    4JWU X-ray 2.20 A/B 1-415 [» ]
    4JX1 X-ray 2.09 A/B/E/F 1-415 [» ]
    4KKY X-ray 2.00 X 2-414 [» ]
    4L49 X-ray 2.13 A 1-415 [» ]
    4L4A X-ray 2.10 A 1-415 [» ]
    4L4B X-ray 2.10 A 1-415 [» ]
    4L4C X-ray 2.20 A/B 1-415 [» ]
    4L4D X-ray 2.10 A 1-415 [» ]
    4L4E X-ray 1.26 A 1-415 [» ]
    4L4F X-ray 1.29 A 1-415 [» ]
    4L4G X-ray 1.55 A 1-415 [» ]
    5CP4 X-ray 1.75 A 2-415 [» ]
    5CPP X-ray 2.08 A 2-415 [» ]
    6CP4 X-ray 1.90 A 2-415 [» ]
    6CPP X-ray 1.90 A 2-415 [» ]
    7CPP X-ray 2.00 A 2-415 [» ]
    8CPP X-ray 2.10 A 2-415 [» ]
    ProteinModelPortali P00183.
    SMRi P00183. Positions 10-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29809N.

    Chemistry

    BindingDBi P00183.
    ChEMBLi CHEMBL5594.
    DrugBanki DB01011. Metyrapone.
    DB00184. Nicotine.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00719 .
    BioCyci MetaCyc:MONOMER-3021.

    Miscellaneous databases

    EvolutionaryTracei P00183.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00359. BP450.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli."
      Unger B.P., Gunsalus I.C., Sligar S.G.
      J. Biol. Chem. 261:1158-1163(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: G1 / ATCC 17453.
    2. "Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida."
      Koga H., Yamaguchi E., Matsunaga K., Aramaki H., Horiuchi T.
      J. Biochem. 106:831-836(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 386-415.
      Strain: G1 / ATCC 17453.
    3. "Amino acid sequence of the Pseudomonas putida cytochrome P-450. II. Cyanogen bromide peptides, acid cleavage peptides, and the complete sequence."
      Haniu M., Armes L.G., Yasunobu K.T., Shastry B.A., Gunsalus I.C.
      J. Biol. Chem. 257:12664-12671(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-415.
    4. "P-450 binding to substrates camphor and linalool versus pressure."
      Marden M.C., Hui Bon Hoa G.
      Arch. Biochem. Biophys. 253:100-107(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSORPTION SPECTROSCOPY.
    5. "Dynamic behavior of the active site structure in bacterial cytochrome P-450."
      Jung C., Marlow F.
      Studia Biophys. 120:241-251(1987)
      Cited for: FOURIER-TRANSFORM INFRARED SPECTROSCOPY.
    6. "Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure."
      Hui Bon Hoa G., Di Primo C., Dondaine I., Sligar S.G., Gunsalus I.C., Douzou P.
      Biochemistry 28:651-656(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSORPTION SPECTROSCOPY, FLUORESCENCE SPECTROSCOPY.
    7. "Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450."
      Nolting B., Jung C., Snatzke G.
      Biochim. Biophys. Acta 1100:171-176(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CIRCULAR DICHROISM ANALYSIS.
    8. "Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin."
      Deprez E., Gill E., Helms V., Wade R., Hui Bon Hoa G.
      J. Inorg. Biochem. 91:597-606(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE-PROTEIN INTERACTION.
    9. "The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450."
      Poulos T.L., Finzel B.C., Gunsalus I.C., Wagner G.C., Kraut J.
      J. Biol. Chem. 260:16122-16130(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    10. "Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer."
      Schlichting I., Jung C., Schulze H.
      FEBS Lett. 415:253-257(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    11. "Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein."
      Di Gleria K., Nickerson D.P., Hill H.A.O., Wong L.-L., Fueloep V.
      J. Am. Chem. Soc. 120:46-52(1998)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    12. "Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect."
      Vidakovic M., Sligar S.G., Li H., Poulos T.L.
      Biochemistry 37:9211-9219(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    13. "Optical detection of cytochrome P450 by sensitizer-linked substrates."
      Dmochowski I.J., Crane B.R., Wilker J.J., Winkler J.R., Gray H.B.
      Proc. Natl. Acad. Sci. U.S.A. 96:12987-12990(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    15. "X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center."
      Hishiki T., Shimada H., Nagano S., Egawa T., Kanamori Y., Makino R., Park S.-Y., Adachi S., Shiro Y., Ishimura Y.
      J. Biochem. 128:965-974(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
    16. "Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam."
      Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.
      Biochemistry 40:2669-2677(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    17. "Probing the open state of cytochrome P450cam with ruthenium-linker substrates."
      Dunn A.R., Dmochowski I.J., Bilwes A.M., Gray H.B., Crane B.R.
      Proc. Natl. Acad. Sci. U.S.A. 98:12420-12425(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    18. "Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes."
      Fedorov R., Ghosh D.K., Schlichting I.
      Arch. Biochem. Biophys. 409:25-31(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    19. "1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton."
      Mouro C., Bondon A., Simmoneaux G., Jung C.
      FEBS Lett. 414:203-208(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiCPXA_PSEPU
    AccessioniPrimary (citable) accession number: P00183
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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

    External Data

    Dasty 3