ID A0A0D5M2J6_9GAMM Unreviewed; 463 AA.
AC A0A0D5M2J6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000256|ARBA:ARBA00016603, ECO:0000256|HAMAP-Rule:MF_00247};
DE Short=STH {ECO:0000256|HAMAP-Rule:MF_00247};
DE EC=1.6.1.1 {ECO:0000256|ARBA:ARBA00012772, ECO:0000256|HAMAP-Rule:MF_00247};
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000256|ARBA:ARBA00031183, ECO:0000256|HAMAP-Rule:MF_00247};
GN Name=sthA {ECO:0000256|HAMAP-Rule:MF_00247};
GN ORFNames=KO116_01937 {ECO:0000313|EMBL:AJY50420.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY50420.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY50420.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY50420.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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, ECO:0000256|HAMAP-
CC Rule:MF_00247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + NADPH = NADH + NADP(+); Xref=Rhea:RHEA:11692,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58349; EC=1.6.1.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00247};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00247,
CC ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_00247,
CC ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00247}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|HAMAP-Rule:MF_00247}.
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DR EMBL; CP011052; AJY50420.1; -; Genomic_DNA.
DR RefSeq; WP_035557293.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5M2J6; -.
DR STRING; 1504981.KO116_01937; -.
DR KEGG; hak:KO116_01937; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_0_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006739; P:NADP metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR HAMAP; MF_00247; SthA; 1.
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 InterPro; IPR022962; STH_gammaproteobact.
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, ECO:0000256|HAMAP-Rule:MF_00247};
KW FAD {ECO:0000256|HAMAP-Rule:MF_00247, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00247};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00247};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00247};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00247,
KW ECO:0000313|EMBL:AJY50420.1}.
FT DOMAIN 6..325
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..454
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 35..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00247"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 145..147
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 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 463 AA; 51584 MW; 93D89990B3B1442E CRC64;
MAVHNYDVVV IGTGPAGESA AINAAKHGKR VAIIEKQAQV GGNCTHWGTI PSKALRHQVK
QIMAFNTNRM FRDIGEPRWF SFPKVMERSR GTIDKQVEMR TTFYARNRID LFHGVARFKD
EHTLVVRDRQ EGMEELVAKK IVIATGSRPY RPANINFRHP RIYCSDTILS LSHTPRTLVI
FGAGVIGCEY ASIFSGLGVK VDLINNRDSL LSFLDDEISD ALSYHLRKHG VLVRHNEEYE
SVEGDESGVI VRLKSGKKIR ADAFLWANGR TGNTDSLGLE NIGLNANGRG QLSVDEHYRT
EVPHIYAAGD VIGWPSLASA AYDQGLNSCN ELLDKEYRFV SDVPTGIYTI PEISSFGPNE
RELTEAKVPY EVGKAFFKDT ARAQITGDTV GMLKILFHQD TLEILGIHCF GDQASEILHI
GQAIMQQEGE ANTLNYFVNT TFNYPTMAEA YRVAAQNGLN RVF
//
