ID PNTAB_RHORT Reviewed; 139 AA. AC Q2RSB3; Q59762; Q59764; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=NAD(P) transhydrogenase subunit alpha part 2; DE EC=1.6.1.2; DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha 2; DE AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha 2; DE AltName: Full=Proton-translocating transhydrogenase component 2; DE AltName: Full=dII; GN Name=pntAB; Synonyms=nntA2; OrderedLocusNames=Rru_A2182; OS Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94356221; PubMed=8075801; RA Williams R., Cotton N.P., Thomas C.M., Jackson J.B.; RT "Cloning and sequencing of the genes for the proton-translocating RT nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum RT and the implications for the domain structure of the enzyme."; RL Microbiology 140:1595-1604(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled CC to respiration and ATP hydrolysis and functions as a proton pump CC across the membrane (By similarity). CC -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH. CC -!- SUBUNIT: Complex of an alpha and a beta chain; in Rhodospirillum, CC the alpha chain seems to be made of two subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein (By similarity). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U05294; AAA62494.1; -; Genomic_DNA. DR EMBL; CP000230; ABC22982.1; -; Genomic_DNA. DR RefSeq; YP_427269.1; -. DR GeneID; 3835609; -. DR GenomeReviews; CP000230_GR; Rru_A2182. DR KEGG; rru:Rru_A2182; -. DR NMPDR; fig|1085.1.peg.3657; -. DR HOGENOM; Q2RSB3; -. DR OMA; Q2RSB3; LALQASH. DR BioCyc; RRUB269796:RRU_A2182-MON; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) acti...; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW NADP; Oxidoreductase; Transmembrane. FT CHAIN 1 139 NAD(P) transhydrogenase subunit alpha FT part 2. FT /FTId=PRO_0000231664. FT TRANSMEM 49 69 Potential. FT TRANSMEM 78 98 Potential. FT TRANSMEM 107 127 Potential. SQ SEQUENCE 139 AA; 14889 MW; 04742D87817A8879 CRC64; MEDKNILVEG FNQLSQQALE LSQHAQALAL QASHAVLPAA AATEGASEFW WLMTVFVLAC FIGFYVVWSV TPALHSPLMG VTNAISSVIV VGALIATGPE AFSASKVLGF FAILLASVNI FGGFIVTQRM LAMFKKKQK //