ID A0A2N0VM51_9BACT Unreviewed; 483 AA.
AC A0A2N0VM51;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CWD77_07485 {ECO:0000313|EMBL:PKD45276.1};
OS Rhodohalobacter barkolensis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2053187 {ECO:0000313|EMBL:PKD45276.1, ECO:0000313|Proteomes:UP000233398};
RN [1] {ECO:0000313|EMBL:PKD45276.1, ECO:0000313|Proteomes:UP000233398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15182 {ECO:0000313|EMBL:PKD45276.1,
RC ECO:0000313|Proteomes:UP000233398};
RA Han S.;
RT "Rhodohalobacter 15182 sp. nov., isolated from a salt lake.";
RL Submitted (NOV-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|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:PKD45276.1}.
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DR EMBL; PISP01000001; PKD45276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0VM51; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000233398; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000233398}.
FT DOMAIN 5..333
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 352..460
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 146..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 183..190
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 483 AA; 54036 MW; BDA24718CC62F8AB CRC64;
MSFDYDVIII GSGPAGFSCA MQSTKFDKKV LIVEADDNHL GGTWLNKGTV PSKALREAAD
LIQDFHTQFG DEKGRKPFER FRMEDLLSYK KSALDSKNRK VKTDLIKNEV ETARGWGEIV
DEHTVTVKDS LNKTTTYTTE NILIATGSRP EEPKNFNIDH SSVLDYNSIL NITHIPRRLV
IVGSGVISFE YATIFASLGT RITILNDSDE FLPFLDHEIR DDVFKVLKKK GIIIHTLSKV
KEVKPNPLRT CMEVVFRSEL EDRLQVLESD HILYVGGKIP NTDNLFDSTL NIDLNDEGYI
NTDHHYRTAV KNIYAAGDVT GDPTSASASF VQGRLAACSM FDIPSESPTG DIPYGIYSIP
EISGIGLTEE QAHDMGIDVT VGRAYYKNLT YADINHRTDG MLKLVFKTDD LKLLGVHIFG
DHATDLIHLG QSIMAQDGTI KYFIEHVLNY PTYSEAYRVA AFNGVNRVYK AGVKYKNILN
NKS
//
