ID   TERPA_PSESP             Reviewed;         409 AA.
AC   P33009;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Terpredoxin reductase;
DE            EC=1.18.1.-;
GN   Name=terPA;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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=FAD; Xref=ChEBI:CHEBI:57692;
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DR   EMBL; M91440; AAA25997.1; -; Genomic_DNA.
DR   PIR; D42971; D42971.
DR   AlphaFoldDB; P33009; -.
DR   SMR; P33009; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   4: Predicted;
KW   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..409
FT                   /note="Terpredoxin reductase"
FT                   /id="PRO_0000167648"
FT   BINDING         7..38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         151..159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   409 AA;  44355 MW;  C9B032ABCF651C88 CRC64;
     MGERRDTTVI VGAGHAGTAA AFFLREFGYH GRVLLLSAET QHPYQRPPLS KEYLLAQHST
     PSLLKGKDSY ARADIELCLQ DDVLSITPAS RQVKSSQGSY TYDHLILATG SHPRFMATLG
     QADNLCYLSD WDDAGRIRQQ LGEASRIVVL GGGFIGLEIA SSACKMGKHV TVIERAPRLL
     SRVVSEAFAT FIGDIHLGNG IELRLGEEVR EVRRCTSGVR VDAVFLSDGQ LLECDMLVIG
     VGSEPRMELA TAAGLACASG VLVDEHCHTS DPFISAIGDC VAVCPSPGHQ LPRRESVQNA
     TEQARLVAAR LSGRPVPPVQ TPWFWSDQLQ ARINLAGERP AQGQVIVRRY GGDKVSMLYL
     QDQQLVAIEA CNMPGDCLLA RRAIGQNHSL DLARLVDADV PLKDALHFA