位置:首页 > 蛋白库 > STHA_ALIF1
STHA_ALIF1
ID   STHA_ALIF1              Reviewed;         471 AA.
AC   Q5E212;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000255|HAMAP-Rule:MF_00247};
DE            Short=STH {ECO:0000255|HAMAP-Rule:MF_00247};
DE            EC=1.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00247};
DE   AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000255|HAMAP-Rule:MF_00247};
GN   Name=sthA {ECO:0000255|HAMAP-Rule:MF_00247}; OrderedLocusNames=VF_2439;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for energy
CC       generation. {ECO:0000255|HAMAP-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:0000255|HAMAP-
CC         Rule:MF_00247};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00247};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00247};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00247}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000255|HAMAP-Rule:MF_00247}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW86934.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; CP000020; AAW86934.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_017019516.1; NC_006840.2.
DR   RefSeq; YP_205822.1; NC_006840.2.
DR   AlphaFoldDB; Q5E212; -.
DR   SMR; Q5E212; -.
DR   STRING; 312309.VF_2439; -.
DR   EnsemblBacteria; AAW86934; AAW86934; VF_2439.
DR   KEGG; vfi:VF_2439; -.
DR   PATRIC; fig|312309.11.peg.2467; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   OrthoDB; 267896at2; -.
DR   Proteomes; UP000000537; Chromosome I.
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: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   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..471
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_0000260245"
FT   BINDING         41..50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00247"
SQ   SEQUENCE   471 AA;  51674 MW;  A9AE438FF166DD15 CRC64;
     MTNSTPIRST HFDAIVIGSG PGGEGAAMGL TKANLNVAII EREPSVGGGC THWGTIPSKA
     LRHAVSRIIE FNSNPLYCKN NTSLHSTFSD ILGHAKSVID KQTRMRQGFY DRNQCSLIFG
     EASFVEKNTV AVTAKDGSIE TYTADKFIIA TGSRPYRPEG INFNHSRVYD SDSILSLKHD
     PRHIIIYGAG VIGSEYASIF RGLGVKVDLV NTRDRLLSFL DNEMSDALSY HFWNSGIVTR
     NDENFEHIEA NDDGVIMHLE SGKKMKADCI LFANGRTGNT DKLNLSAVGL EADSRGQLKV
     NDNYQTDVEH IYAVGDVIGY PSLASAAYDQ GRFTAQAITK GKAEARLIDH IPTGIYTIPE
     ISSVGKTEQE LTAAKVPYEV GRSSFKHLAR AQIAGKDIGS LKILFHRETK EILGIHCFGE
     RAAEIIHIGQ AIMEQKGEAN TIEYFVNTTF NYPTMAEAYR VAALNGLNRL F
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025