TERPB_PSESP
ID TERPB_PSESP Reviewed; 106 AA.
AC P33007;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Terpredoxin;
DE Short=TDX;
GN Name=terPB;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24.
RX PubMed=1629218; DOI=10.1016/s0021-9258(19)49697-x;
RA Peterson J.A., Lu J.-Y., Geisselsoder J., Graham-Lorence S., Carmona C.,
RA Witney F., Lorence M.C.;
RT "Cytochrome P-450terp. Isolation and purification of the protein and
RT cloning and sequencing of its operon.";
RL J. Biol. Chem. 267:14193-14203(1992).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=10220356; DOI=10.1021/bi983063r;
RA Mo H., Pochapsky S.S., Pochapsky T.C.;
RT "A model for the solution structure of oxidized terpredoxin, a Fe2S2
RT ferredoxin from Pseudomonas.";
RL Biochemistry 38:5666-5675(1999).
CC -!- FUNCTION: The oxidation of alpha-terpineol by cytochrome p450-TERP
CC requires the participation of a flavoprotein, terpredoxin reductase,
CC and an iron-sulfur protein, terpredoxin, to mediate the transfer of
CC electrons 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 -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; M91440; AAA25998.1; -; Genomic_DNA.
DR PIR; E42971; E42971.
DR PDB; 1B9R; NMR; -; A=2-106.
DR PDBsum; 1B9R; -.
DR AlphaFoldDB; P33007; -.
DR SMR; P33007; -.
DR EvolutionaryTrace; P33007; -.
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:1629218"
FT CHAIN 2..106
FT /note="Terpredoxin"
FT /id="PRO_0000201164"
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 BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1B9R"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1B9R"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1B9R"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:1B9R"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1B9R"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1B9R"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:1B9R"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1B9R"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1B9R"
SQ SEQUENCE 106 AA; 11229 MW; 38E67F582B649174 CRC64;
MPRVVFIDEQ SGEYAVDAQD GQSLMEVATQ NGVPGIVAEC GGSCVCATCR IEIEDAWVEI
VGEANPDEND LLQSTGEPMT AGTRLSCQVF IDPSMDGLIV RVPLPA