ID L7V6G2_MYCL1 Unreviewed; 468 AA.
AC L7V6G2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=sthA {ECO:0000313|EMBL:AGC62053.1};
GN OrderedLocusNames=MULP_02170 {ECO:0000313|EMBL:AGC62053.1};
OS Mycobacterium liflandii (strain 128FXT).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=459424 {ECO:0000313|EMBL:AGC62053.1, ECO:0000313|Proteomes:UP000011157};
RN [1] {ECO:0000313|EMBL:AGC62053.1, ECO:0000313|Proteomes:UP000011157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128FXT {ECO:0000313|EMBL:AGC62053.1,
RC ECO:0000313|Proteomes:UP000011157};
RX PubMed=23204453; DOI=10.1128/JB.02132-12;
RA Tobias N.J., Doig K.D., Medema M.H., Chen H., Haring V., Moore R.,
RA Seemann T., Stinear T.P.;
RT "Complete Genome Sequence of the Frog Pathogen Mycobacterium ulcerans
RT Ecovar Liflandii.";
RL J. Bacteriol. 195:556-564(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003899; AGC62053.1; -; Genomic_DNA.
DR AlphaFoldDB; L7V6G2; -.
DR KEGG; mli:MULP_02170; -.
DR PATRIC; fig|459424.11.peg.2230; -.
DR HOGENOM; CLU_016755_0_0_11; -.
DR Proteomes; UP000011157; Chromosome.
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:AGC62053.1}.
FT DOMAIN 4..325
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 345..452
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 182..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 468 AA; 50679 MW; 4AB8FED09DF1F7E8 CRC64;
MREYDMVVIG SGPGGQKAAI ASAKLGKSVA IIERGRMLGG VCVNTGTIPS KTLREAVLYL
TGMNQRELYG ASYRVKDRIT PADLLARTQH VIGKEVDVVR NQLMRNRVDL IVGHGRFVDP
HSIVVEDQTH REKTTVTGDY IVIATGTRPA RPSGVEFDED KVLDSNGILD LKSLPASMVV
VGAGVIGIEY ASMFAALGTK VTVVEKRDNM LDFCDPEVVE ALKFHLRDLA VTFRFGEEVT
AVDVGSAGTV TTLASGKQIP AETVMYSAGR QGQTDHLDLA NAGLEVEGRG RIWVDDKFRT
KVEHIYAVGD VIGFPALAAT SMEQGRLAAY HAFGEPTDGI TELQPIGIYS IPEISYVGAT
EVELTKNSIP YEVGVARYRE LARGQIAGDS YGMLKLLVST EDLTLLGVHI FGTSATEMVH
IGQAIMGCGG TVEYLVEAVF NYPTFSEAYK VAALDVMNKV RALNQFRR
//
