ID PNTB_ECOL6 Reviewed; 462 AA. AC P0AB68; P07002; P76890; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 04-NOV-2026, entry version 107. DE RecName: Full=NAD(P) transhydrogenase subunit beta; DE EC=7.1.1.1; DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; DE AltName: Full=Pyridine nucleotide transhydrogenase subunit beta; GN Name=pntB; OrderedLocusNames=c1994; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to CC respiration and ATP hydrolysis and functions as a proton pump across CC the membrane. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + NADPH + H(+)(in) = NADH + NADP(+) + H(+)(out); CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1; CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PNT beta subunit family. {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; AE014075; AAN80454.1; -; Genomic_DNA. DR RefSeq; WP_000014036.1; NC_004431.1. DR AlphaFoldDB; P0AB68; -. DR BMRB; P0AB68; -. DR SMR; P0AB68; -. DR STRING; 199310.c1994; -. DR GeneID; 93775750; -. DR KEGG; ecc:c1994; -. DR eggNOG; COG1282; Bacteria. DR HOGENOM; CLU_007866_4_0_6; -. DR OMA; AADNHLM; -. DR BioCyc; ECOL199310:C1994-MONOMER; -. DR Proteomes; UP000001410; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0008750; F:proton-translocating NAD(P)+ transhydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:UniProtKB-ARBA. DR FunFam; 3.40.50.1220:FF:000002; NAD(P) transhydrogenase subunit beta; 1. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR012136; NADH_DH_b. DR InterPro; IPR034300; PNTB-like. DR NCBIfam; NF006974; pntB; 1. DR PANTHER; PTHR44758; NAD(P) TRANSHYDROGENASE SUBUNIT BETA; 1. DR PANTHER; PTHR44758:SF1; NAD(P) TRANSHYDROGENASE SUBUNIT BETA; 1. DR Pfam; PF02233; PNTB; 1. DR PIRSF; PIRSF000204; PNTB; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Membrane; NAD; NADP; KW Reference proteome; Translocase; Transmembrane; Transmembrane helix. FT CHAIN 1..462 FT /note="NAD(P) transhydrogenase subunit beta" FT /id="PRO_0000199025" FT TOPO_DOM 1..3 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 4..24 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 25..45 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 46..66 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 67..82 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 104..115 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 116..136 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 137..164 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 186..188 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 210..215 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 216..236 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 237..239 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 240..260 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 261..308 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 309..329 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 330..462 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" SQ SEQUENCE 462 AA; 48723 MW; D11747291D271A2F CRC64; MSGGLVTAAY IVAAILFIFS LAGLSKHETS RQGNNFGIAG MAIALIATIF GPDTGNVGWI LLAMVIGGAI GIRLAKKVEM TEMPELVAIL HSFVGLAAVL VGFNSYLHHD AGMAPILVNI HLTEVFLGIF IGAVTFTGSV VAFGKLCGKI SSKPLMLPNR HKMNLAALVV SFLLLIVFVR TDSVGLQVLA LLIMTAIALV FGWHLVASIG GADMPVVVSM LNSYSGWAAA AAGFMLSNDL LIVTGALVGS SGAILSYIMC KAMNRSFISV IAGGFGTDGS STGDDQEVGE HREITAEETA ELLKNSHSVI ITPGYGMAVA QAQYPVAEIT EKLRARGINV RFGIHPVAGR LPGHMNVLLA EAKVPYDIVL EMDEINDDFA DTDTVLVIGA NDTVNPAAQD DPKSPIAGMP VLEVWKAQNV IVFKRSMNTG YAGVQNPLFF KENTHMLFGD AKASVDAILK AL //