CAMA_PSEPU
ID CAMA_PSEPU Reviewed; 422 AA.
AC P16640;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putidaredoxin reductase CamA {ECO:0000303|PubMed:3003058};
DE Short=Pdr {ECO:0000303|PubMed:12011076};
DE EC=1.18.1.5 {ECO:0000269|PubMed:12011076};
DE AltName: Full=Putidaredoxin--NAD(+) reductase {ECO:0000303|PubMed:2613690};
GN Name=camA {ECO:0000303|PubMed:3003058};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=G1 / ATCC 17453;
RX PubMed=2613690; DOI=10.1093/oxfordjournals.jbchem.a122939;
RA Koga H., Yamaguchi E., Matsunaga K., Aramaki H., Horiuchi T.;
RT "Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene
RT (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam
RT hydroxylase of Pseudomonas putida.";
RL J. Biochem. 106:831-836(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G1 / ATCC 17453;
RX PubMed=2180940; DOI=10.1016/s0021-9258(19)39292-0;
RA Peterson J.A., Lorence M.C., Amarneh B.;
RT "Putidaredoxin reductase and putidaredoxin. Cloning, sequence
RT determination, and heterologous expression of the proteins.";
RL J. Biol. Chem. 265:6066-6073(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RX PubMed=3003058; DOI=10.1016/s0021-9258(17)36068-4;
RA Unger B.P., Gunsalus I.C., Sligar S.G.;
RT "Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and
RT its expression in Escherichia coli.";
RL J. Biol. Chem. 261:1158-1163(1986).
RN [4]
RP CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
RX PubMed=12011076; DOI=10.1074/jbc.m201110200;
RA Sevrioukova I.F., Poulos T.L.;
RT "Putidaredoxin reductase, a new function for an old protein.";
RL J. Biol. Chem. 277:25831-25839(2002).
RN [5]
RP INTERACTION WITH PUTIDAREDOXIN CAMB.
RX PubMed=11524002; DOI=10.1021/bi010874d;
RA Sevrioukova I.F., Hazzard J.T., Tollin G., Poulos T.L.;
RT "Laser flash induced electron transfer in P450cam monooxygenase:
RT putidaredoxin reductase-putidaredoxin interaction.";
RL Biochemistry 40:10592-10600(2001).
RN [6]
RP INTERACTION WITH PUTIDAREDOXIN CAMB.
RX PubMed=15716266; DOI=10.1074/jbc.m500771200;
RA Kuznetsov V.Y., Blair E., Farmer P.J., Poulos T.L., Pifferitti A.,
RA Sevrioukova I.F.;
RT "The putidaredoxin reductase-putidaredoxin electron transfer complex:
RT theoretical and experimental studies.";
RL J. Biol. Chem. 280:16135-16142(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15095867; DOI=10.1016/j.jmb.2003.12.067;
RA Sevrioukova I.F., Li H., Poulos T.L.;
RT "Crystal structure of putidaredoxin reductase from Pseudomonas putida, the
RT final structural component of the cytochrome P450cam monooxygenase.";
RL J. Mol. Biol. 336:889-902(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PUTIDAREDOXIN CAMB
RP AND FAD, AND COFACTOR.
RX PubMed=20179327; DOI=10.1074/jbc.m110.104968;
RA Sevrioukova I.F., Poulos T.L., Churbanova I.Y.;
RT "Crystal structure of the putidaredoxin reductase x putidaredoxin electron
RT transfer complex.";
RL J. Biol. Chem. 285:13616-13620(2010).
CC -!- FUNCTION: The oxidation of camphor by cytochrome P450-CAM CamC requires
CC the participation of the flavoprotein, putidaredoxin reductase CamA,
CC and the iron-sulfur protein, putidaredoxin CamB, to mediate the
CC transfer of electrons from NADH to P450 for oxygen activation.
CC {ECO:0000269|PubMed:12011076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[putidaredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[putidaredoxin]; Xref=Rhea:RHEA:33063, Rhea:RHEA-
CC COMP:14157, Rhea:RHEA-COMP:14158, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.5;
CC Evidence={ECO:0000269|PubMed:12011076};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12011076, ECO:0000269|PubMed:15095867,
CC ECO:0000269|PubMed:20179327};
CC -!- PATHWAY: Terpene metabolism; (R)-camphor degradation.
CC -!- SUBUNIT: Homodimer or monomer. {ECO:0000269|PubMed:15095867}.
CC -!- INDUCTION: Induced by camphor and repressed by CamR.
CC {ECO:0000269|PubMed:2613690}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; D00528; BAA00413.1; -; Genomic_DNA.
DR EMBL; J05406; AAA25758.1; -; Genomic_DNA.
DR EMBL; M12546; AAA25761.1; -; Genomic_DNA.
DR PIR; JX0078; JX0078.
DR PDB; 1Q1R; X-ray; 1.91 A; A/B=1-422.
DR PDB; 1Q1W; X-ray; 2.60 A; A/B=1-422.
DR PDB; 3LB8; X-ray; 2.60 A; A/B=2-422.
DR PDBsum; 1Q1R; -.
DR PDBsum; 1Q1W; -.
DR PDBsum; 3LB8; -.
DR AlphaFoldDB; P16640; -.
DR SMR; P16640; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR KEGG; ag:AAA25758; -.
DR BioCyc; MetaCyc:MON-3501; -.
DR BRENDA; 1.18.1.5; 5092.
DR UniPathway; UPA00719; -.
DR EvolutionaryTrace; P16640; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019383; P:(+)-camphor catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..422
FT /note="Putidaredoxin reductase CamA"
FT /id="PRO_0000167646"
FT BINDING 15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:1Q1W, ECO:0007744|PDB:3LB8"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:1Q1W, ECO:0007744|PDB:3LB8"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:1Q1W, ECO:0007744|PDB:3LB8"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:1Q1W, ECO:0007744|PDB:3LB8"
FT BINDING 134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:3LB8"
FT BINDING 156..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:3LB8"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15095867,
FT ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R,
FT ECO:0007744|PDB:3LB8"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1Q1R"
FT TURN 49..55
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1Q1R"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1Q1R"
FT TURN 184..188
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1Q1R"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:1Q1R"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1Q1R"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:1Q1R"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:1Q1R"
FT HELIX 408..421
FT /evidence="ECO:0007829|PDB:1Q1R"
SQ SEQUENCE 422 AA; 45579 MW; 704BF52E47491AD1 CRC64;
MNANDNVVIV GTGLAGVEVA FGLRASGWEG NIRLVGDATV IPHHLPPLSK AYLAGKATAE
SLYLRTPDAY AAQNIQLLGG TQVTAINRDR QQVILSDGRA LDYDRLVLAT GGRPRPLPVA
SGAVGKANNF RYLRTLEDAE CIRRQLIADN RLVVIGGGYI GLEVAATAIK ANMHVTLLDT
AARVLERVTA PPVSAFYEHL HREAGVDIRT GTQVCGFEMS TDQQKVTAVL CEDGTRLPAD
LVIAGIGLIP NCELASAAGL QVDNGIVINE HMQTSDPLIM AVGDCARFHS QLYDRWVRIE
SVPNALEQAR KIAAILCGKV PRDEAAPWFW SDQYEIGLKM VGLSEGYDRI IVRGSLAQPD
FSVFYLQGDR VLAVDTVNRP VEFNQSKQII TDRLPVEPNL LGDESVPLKE IIAAAKAELS
SA
