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 13-SEP-2023, entry version 126. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:MONOMER-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; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1. DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF14759; Reductase_C; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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 //