ID   A9CIS9_AGRFC            Unreviewed;       467 AA.
AC   A9CIS9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000256|ARBA:ARBA00016603};
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:AAK87434.2};
GN   OrderedLocusNames=Atu1661 {ECO:0000313|EMBL:AAK87434.2};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
OC   Agrobacterium; Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK87434.2, ECO:0000313|Proteomes:UP000000813};
RN   [1] {ECO:0000313|EMBL:AAK87434.2, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2] {ECO:0000313|EMBL:AAK87434.2, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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}.
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DR   EMBL; AE007869; AAK87434.2; -; Genomic_DNA.
DR   RefSeq; WP_010971781.1; NC_003062.2.
DR   AlphaFoldDB; A9CIS9; -.
DR   STRING; 176299.Atu1661; -.
DR   EnsemblBacteria; AAK87434; AAK87434; Atu1661.
DR   GeneID; 1133699; -.
DR   KEGG; atu:Atu1661; -.
DR   PATRIC; fig|176299.10.peg.1679; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_5; -.
DR   OMA; AAHHMWS; -.
DR   OrthoDB; 9781772at2; -.
DR   PhylomeDB; A9CIS9; -.
DR   Proteomes; UP000000813; Chromosome circular.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase (NADH) activity; IEA:TreeGrafter.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:TreeGrafter.
DR   GO; GO:0003957; F:NAD(P)+ transhydrogenase (Si-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:TreeGrafter.
DR   FunFam; 3.30.390.30:FF:000001; Dihydrolipoyl dehydrogenase; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR050151; Class-I_Pyr_Nuc-Dis_Oxidored.
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   NCBIfam; NF003585; sthA; 1.
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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000813}.
FT   DOMAIN          4..326
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          346..451
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         181..188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         204
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         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ   SEQUENCE   467 AA;  51369 MW;  775612541DA80783 CRC64;
     MYQFDLIVVG SGPAGRRAAI QAAKLEKKVL VIEKGSRVGG VSVHTGTIPS KTLRETALNL
     TGWRERGFYG RAYRVKQEID ADDLRRRLLI TLDHEVEVLE HQFARNRVQH IRGTASFIDA
     NTMKVVKSDG EVMTVTATSI LLTIGTRPYR PPHIPFDGQA VLDSDEILEI KELPRSMVVV
     GAGVIGIEYA TIFSALDTQV TVVEPRETML EFIDKEIVED FTYQLRDRNM KLIFGQKAEK
     VERDESGKCL VSLSNGRVLK AETVLFAAGR VGATDTLNLS ACGLEADSRG RLKVDPETFQ
     TSVPNIYAAG DIIGFPSLAS TSMEQGRIAA RHAVGAPAGE PPQFFPYGIY AVPEISTCGL
     TEEEVVERGI PYECGIAHFR ETSRGHIMGL DSGLLKMIFS LKTRRLLGVH IVGEGATELV
     HIGQAVLNLK GTVEYFVENT FNYPTLAEAY KIAGLDAWNR MGELKKD
//