ID A0A225VHW9_9STRA Unreviewed; 549 AA.
AC A0A225VHW9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=NAD(P)(+) transhydrogenase (Si-specific) {ECO:0000256|ARBA:ARBA00012772};
DE EC=1.6.1.1 {ECO:0000256|ARBA:ARBA00012772};
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000256|ARBA:ARBA00031183};
GN ORFNames=PHMEG_00023072 {ECO:0000313|EMBL:OWZ04935.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ04935.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC pathways, to NADH, which can enter the respiratory chain for energy
CC generation. {ECO:0000256|ARBA:ARBA00002842}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004137};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004137};
CC Intermembrane side {ECO:0000256|ARBA:ARBA00004137}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWZ04935.1}.
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DR EMBL; NBNE01004696; OWZ04935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225VHW9; -.
DR STRING; 4795.A0A225VHW9; -.
DR EnsemblProtists; OWZ04935; OWZ04935; PHMEG_00023072.
DR OrthoDB; 5486966at2759; -.
DR Proteomes; UP000198211; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR22912:SF93; SOLUBLE PYRIDINE NUCLEOTIDE TRANSHYDROGENASE; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000198211};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 451..486
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 549 AA; 61059 MW; 97C178F730B77255 CRC64;
MLTLSFSSVL TADKFLVCVG TRPARRPDIP FDGETIFDSD QLLWGKVKTV PRRLIIVGAG
VVGMEYASMM TIIPGTDVTV IDGRQEILNM ADKEVSEALC YSMSQTGTRF LVGETIKSVE
KTPNGEVFVH LESGKTVVGD GLLYTVGRQG NVEGLNLEAV GITPDKRGRI KVDNNFQTSV
PHIYAAGDII GFPGLASTSM EQGRLASVVM RTSKSLYTKE ISDDKKMDDP DRVRTRMRSG
EVFPFGIYTV PEISMVGKNE QQLTKEQVPY EVGVARYEEL AKGQMLGGVP GFLKIIFCPE
TLKIFGVHAI GEGATEIIHI GQVVMSTGGT LEYFRNAVFN YPTLAEAYRV AALNGLRKIE
RLRDTCDLNE EQIEEIHMIT SLPPKEIHRI RRKYKTFVKS EDMTKDEFYA LPAIAVNPLR
DQLFKSLEVT QAQTIPFAEF AKFVHIFSYS SSQDAKLKAF KIHDFDGDGK ISRDDLRAYC
SLVFPKVSES EGDVAIKSQQ ETQETLIEQV MHEASSAPSR DFLVYNDFVK ASAVVIQSTD
FESRLIVPF
//
