ID A0A067KPK6_JATCU Unreviewed; 537 AA.
AC A0A067KPK6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial {ECO:0000256|PIRNR:PIRNR000362};
DE EC=1.18.1.6 {ECO:0000256|PIRNR:PIRNR000362};
GN ORFNames=JCGZ_07275 {ECO:0000313|EMBL:KDP33704.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP33704.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP33704.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP33704.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized
CC [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000384,
CC ECO:0000256|PIRNR:PIRNR000362};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR000362, ECO:0000256|PIRSR:PIRSR000362-1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR000362}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000362}.
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DR EMBL; KK914539; KDP33704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067KPK6; -.
DR STRING; 180498.A0A067KPK6; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR PANTHER; PTHR48379; GLUTAMATE SYNTHASE CENTRAL-N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48379:SF1; GLUTAMATE SYNTHASE CENTRAL-N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000362};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000362};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000362};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000362};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000362};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT DOMAIN 21..225
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 30
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 197..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 241..242
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 441
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 448..450
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 448
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 537 AA; 59318 MW; 23F27571AF44719D CRC64;
MFLAKTWLSR SFSTLSSHPL RVCVVGSGPA GFYTAEKMLK AHGEAEIDII DRLPTPFGLV
RSGVAPDHPE TKIVINQFSR VVQHERCSFF GNVTLSSSIS LAELRELYHV VILAYGAESD
RNLGIPGEMS CSYAFDICDD YVANRLQLLI SFICMFLQDL LGIHSAREFV WWYNGHPDCK
NLNPDLERTD TAVILGQGNV ALDVARILLR PTAELATTDI ASHALAALEQ SSIRKVYLVG
RRGPVQAACT AKELREVLVI GLWFPDLVSF SELQYWYNLV AGIKDLYIHI KEVDLLKSSE
DEEELKSSRI QRRVYELLSK AAASGPSHPS SGQRELHFVF FQKPDRFLYS GDQTGHVAGV
HFEKTVLKGV GPGKQVAVGT GKFEDLDCGM VLKSIGYKSV PVDGLPFDHQ KGVVPNVGGR
VLTDASGDTT LLENGLYVCG WLKRGPTGII ATNLYCAEET VANILQDLEQ GTLAGATSLS
MPGREGLLEL LDDRNVRVVP FDAWEKIDAE EKRLGVPRNK PREKLTTWED LLKVATE
//
