PUTX_PSEPU
ID PUTX_PSEPU Reviewed; 107 AA.
AC P00259;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putidaredoxin;
DE Short=PDX;
GN Name=camB;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP PROTEIN SEQUENCE OF 2-107.
RX PubMed=4833743; DOI=10.1016/s0021-9258(19)42529-5;
RA Tanaka M., Haniu M., Yasunobu K.T., Dus K., Gunsalus I.C.;
RT "The amino acid sequence of putidaredoxin, an iron-sulfur protein from
RT Pseudomonas putida.";
RL J. Biol. Chem. 249:3689-3701(1974).
RN [4]
RP INTERACTION WITH PUTIDAREDOXIN REDUCTASE.
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 [5]
RP INTERACTION WITH PUTIDAREDOXIN REDUCTASE.
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANTS.
RX PubMed=14529624; DOI=10.1016/j.jmb.2003.08.028;
RA Sevrioukova I.F., Garcia C., Li H., Bhaskar B., Poulos T.L.;
RT "Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam
RT monooxygenase system from Pseudomonas putida.";
RL J. Mol. Biol. 333:377-392(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT GLY-74.
RX PubMed=15103126; DOI=10.1107/s0907444904003348;
RA Smith N., Mayhew M., Holden M.J., Kelly H., Robinson H., Heroux A.,
RA Vilker V.L., Gallagher D.T.;
RT "Structure of C73G putidaredoxin from Pseudomonas putida.";
RL Acta Crystallogr. D 60:816-822(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF MUTANTS SER-74 AND SER-86.
RX PubMed=15755454; DOI=10.1016/j.jmb.2005.01.047;
RA Sevrioukova I.F.;
RT "Redox-dependent structural reorganization in putidaredoxin, a vertebrate-
RT type [2Fe-2S] ferredoxin from Pseudomonas putida.";
RL J. Mol. Biol. 347:607-621(2005).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=2018758; DOI=10.1021/bi00230a007;
RA Pochapsky T.C., Ye X.M.;
RT "1H NMR identification of a beta-sheet structure and description of folding
RT topology in putidaredoxin.";
RL Biochemistry 30:3850-3856(1991).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=1536837; DOI=10.1021/bi00122a009;
RA Ye X.M., Pochapsky T.C., Pochapsky S.S.;
RT "1H NMR sequential assignments and identification of secondary structural
RT elements in oxidized putidaredoxin, an electron-transfer protein from
RT Pseudomonas.";
RL Biochemistry 31:1961-1968(1992).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=8204575; DOI=10.1021/bi00187a006;
RA Pochapsky T.C., Ye X.M., Ratnaswamy G., Lyons T.A.;
RT "An NMR-derived model for the solution structure of oxidized putidaredoxin,
RT a 2-Fe, 2-S ferredoxin from Pseudomonas.";
RL Biochemistry 33:6424-6432(1994).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=8204576; DOI=10.1021/bi00187a007;
RA Pochapsky T.C., Ratnaswamy G., Patera A.;
RT "Redox-dependent 1H NMR spectral features and tertiary structural
RT constraints on the C-terminal region of putidaredoxin.";
RL Biochemistry 33:6433-6441(1994).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=9835048; DOI=10.1023/a:1008354113765;
RA Pochapsky T.C., Kuti M., Kazanis S.;
RT "The solution structure of a gallium-substituted putidaredoxin mutant:
RT GaPdx C85S.";
RL J. Biomol. NMR 12:407-415(1998).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=10200155; DOI=10.1021/bi983030b;
RA Pochapsky T.C., Jain N.U., Kuti M., Lyons T.A., Heymont J.;
RT "A refined model for the solution structure of oxidized putidaredoxin.";
RL Biochemistry 38:4681-4690(1999).
CC -!- FUNCTION: The oxidation of camphor by cytochrome P450-CAM requires the
CC participation of a flavoprotein, putidaredoxin reductase, and an iron-
CC sulfur protein, putidaredoxin, to mediate the transfer of electrons
CC from NADH to P450 for oxygen activation.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P00259; P00183: camC; NbExp=3; IntAct=EBI-15706395, EBI-15706256;
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; J05406; AAA25759.1; -; Genomic_DNA.
DR EMBL; D00528; BAA00414.1; -; Genomic_DNA.
DR PIR; JX0079; PXPSEP.
DR PDB; 1GPX; NMR; -; A=2-107.
DR PDB; 1OQQ; X-ray; 1.47 A; A/B=2-107.
DR PDB; 1OQR; X-ray; 1.65 A; A/B/C=2-107.
DR PDB; 1PDX; NMR; -; A=2-107.
DR PDB; 1PUT; NMR; -; A=2-107.
DR PDB; 1R7S; X-ray; 1.91 A; A/B/C=2-107.
DR PDB; 1XLN; X-ray; 2.03 A; A/B=2-107.
DR PDB; 1XLO; X-ray; 1.84 A; A/B=2-107.
DR PDB; 1XLP; X-ray; 2.00 A; A/B/C=2-107.
DR PDB; 1XLQ; X-ray; 1.45 A; A/B/C=2-107.
DR PDB; 1YJI; NMR; -; A=2-107.
DR PDB; 1YJJ; NMR; -; A=2-107.
DR PDB; 2M56; NMR; -; B=2-107.
DR PDB; 3LB8; X-ray; 2.60 A; C/D=2-107.
DR PDB; 3W9C; X-ray; 2.50 A; B=2-107.
DR PDB; 4JWS; X-ray; 2.15 A; C/D=2-107.
DR PDB; 4JWU; X-ray; 2.20 A; C/D=1-107.
DR PDB; 4JX1; X-ray; 2.09 A; C/D/G/H=1-107.
DR PDB; 5GXG; X-ray; 1.70 A; B=2-107.
DR PDB; 6NBL; X-ray; 2.15 A; C/D=2-107.
DR PDBsum; 1GPX; -.
DR PDBsum; 1OQQ; -.
DR PDBsum; 1OQR; -.
DR PDBsum; 1PDX; -.
DR PDBsum; 1PUT; -.
DR PDBsum; 1R7S; -.
DR PDBsum; 1XLN; -.
DR PDBsum; 1XLO; -.
DR PDBsum; 1XLP; -.
DR PDBsum; 1XLQ; -.
DR PDBsum; 1YJI; -.
DR PDBsum; 1YJJ; -.
DR PDBsum; 2M56; -.
DR PDBsum; 3LB8; -.
DR PDBsum; 3W9C; -.
DR PDBsum; 4JWS; -.
DR PDBsum; 4JWU; -.
DR PDBsum; 4JX1; -.
DR PDBsum; 5GXG; -.
DR PDBsum; 6NBL; -.
DR AlphaFoldDB; P00259; -.
DR BMRB; P00259; -.
DR SMR; P00259; -.
DR DIP; DIP-29810N; -.
DR IntAct; P00259; 1.
DR BioCyc; MetaCyc:MON-3502; -.
DR EvolutionaryTrace; P00259; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4833743"
FT CHAIN 2..107
FT /note="Putidaredoxin"
FT /id="PRO_0000201162"
FT DOMAIN 2..106
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8204575"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8204575"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8204575"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8204575"
FT CONFLICT 15
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1XLQ"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3LB8"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1XLQ"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3LB8"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1XLQ"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1XLN"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1GPX"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1XLQ"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1XLQ"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1XLQ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1XLQ"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1XLQ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1PUT"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1XLQ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1XLQ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1XLQ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1XLQ"
SQ SEQUENCE 107 AA; 11550 MW; F487E481F8BEE2C9 CRC64;
MSKVVYVSHD GTRRELDVAD GVSLMQAAVS NGIYDIVGDC GGSASCATCH VYVNEAFTDK
VPAANEREIG MLECVTAELK PNSRLCCQII MTPELDGIVV DVPDRQW
