ID A0A3M8FVM6_9BACT Unreviewed; 471 AA.
AC A0A3M8FVM6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=ED559_09485 {ECO:0000313|EMBL:RNC81993.1};
OS Phycisphaera sp.
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=2030824 {ECO:0000313|EMBL:RNC81993.1, ECO:0000313|Proteomes:UP000270436};
RN [1] {ECO:0000313|EMBL:RNC81993.1, ECO:0000313|Proteomes:UP000270436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin4 {ECO:0000313|EMBL:RNC81993.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-2018) 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|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:RNC81993.1}.
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DR EMBL; RHLH01000001; RNC81993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8FVM6; -.
DR Proteomes; UP000270436; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
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; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:RNC81993.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270436}.
FT DOMAIN 4..333
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 353..460
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 180..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 471 AA; 50531 MW; DD1CD40DCAA7A300 CRC64;
MKQYDLCVIG SGPAGQRAAI QAAKLGKRVC VVEKRHAIGG VAVNTGTIPS KALREAILDV
GDRSVACPTM DDFAAVRKTL FANLKRSCSR VIGNEIETIE DHFASNNIDV AHGTGSFSDP
KTIRIETEND ESFIKADYTL IAVGTFPAQP NGVQFDGRTI LSSDDIQEMT AAPHSMIVVG
GGVIGTEYAS MLQALGVKVT LIEGRQRLLD FVDSEIIEAF QYHVRQNGMT LRLGEKVTKI
EVIDAVAGAR TTDGTMAEAH LESGKTLRAD TLLYCIGRQG ATHTLSLENA GLEADKRGRI
GVNESFQTTT PHIYAAGDVI GFPALASTSY EQGRLAACHM FGQSCESISK LLPYGIYAVP
EISMVGWTEG QLTAEGIPYE SGIASYKEIS RGHLLGAEFG MLKMLIHQES HTVLGVHAIG
TGATELIHIG QAAIAFRATV EYFVNAVFNY PTLAECYKVA AMNGLNKLRG I
//
