STHA_PSEAE
ID STHA_PSEAE Reviewed; 464 AA.
AC P57112;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Soluble pyridine nucleotide transhydrogenase;
DE Short=STH;
DE EC=1.6.1.1;
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific];
GN Name=sthA; Synonyms=sth; OrderedLocusNames=PA2991;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP CHARACTERIZATION.
RX PubMed=823872; DOI=10.1016/0003-9861(76)90149-1;
RA Wermuth B., Kaplan N.O.;
RT "Pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa:
RT purification by affinity chromatography and physicochemical properties.";
RL Arch. Biochem. Biophys. 176:136-143(1976).
RN [3]
RP CHARACTERIZATION.
RX PubMed=20086; DOI=10.1016/0006-291x(77)90995-0;
RA Widmer F., Kaplan N.O.;
RT "Pseudomonas aeruginosa transhydrogenase: affinity of substrates for the
RT regulatory site and possible hysteretic behavior.";
RL Biochem. Biophys. Res. Commun. 76:1287-1292(1977).
CC -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC pathways, to NADH, which can enter the respiratory chain for energy
CC generation. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- ACTIVITY REGULATION: Strongly activated by NADPH and 2'-AMP and
CC inhibited by NADP(+). Ca(2+) increases the activation and decreases the
CC inhibition effect.
CC -!- SUBUNIT: Homooligomer; probably composed of four stacked rings of 7 or
CC 8 monomers. Forms filamentous structures.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06379.1; -; Genomic_DNA.
DR PIR; H83271; H83271.
DR RefSeq; NP_251681.1; NC_002516.2.
DR RefSeq; WP_003091177.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; P57112; -.
DR SMR; P57112; -.
DR STRING; 287.DR97_4947; -.
DR PaxDb; P57112; -.
DR PRIDE; P57112; -.
DR EnsemblBacteria; AAG06379; AAG06379; PA2991.
DR GeneID; 878679; -.
DR KEGG; pae:PA2991; -.
DR PATRIC; fig|208964.12.peg.3139; -.
DR PseudoCAP; PA2991; -.
DR HOGENOM; CLU_016755_0_0_6; -.
DR InParanoid; P57112; -.
DR OMA; CLMAVGA; -.
DR PhylomeDB; P57112; -.
DR BioCyc; PAER208964:G1FZ6-3043-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006739; P:NADP metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 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.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..464
FT /note="Soluble pyridine nucleotide transhydrogenase"
FT /id="PRO_0000068068"
FT BINDING 35..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 51161 MW; 886CEAB5479997A9 CRC64;
MAVYNYDVVI LGTGPAGEGA AMNASKYGRK LAVVDSRRVV GGNCTHLGTI PSKALRHSVK
QIIEFNTNPM FRQIGEPRWF SFPDVLKSAD RVISKQVASR TGYYARNRID MFTGTASFVD
ERTVEVVTPS GAVERLVADQ FVIATGSRPY RPSDINFNHP RVYDSDTILS LSHTPRRLII
YGAGVIGCEY ASIFSGLGVL VDLIDTRDQL LSFLDDEISD ALSYHLRNNN VLIRHNEEYE
RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NVGIKVNSRG QIEVDENYRT
SVSNIFAAGD VIGWPSLASA AYDQGRSAAG NIVESDSWRF VNDVPTGIYT IPEISSIGKN
ESELTAAKIP YEVGKAFFKG MARAQISNEP VGMLKILFHR ETLEILGVHC FGDQASEIVH
IGQAIMNQPG ELNTLKYFVN TTFNYPTMAE AYRVAAFDGL NRLF
