PNTB_RHORT
ID PNTB_RHORT Reviewed; 464 AA.
AC Q2RSB4; Q59763; Q59765;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Proton-translocating transhydrogenase NADP(H)-binding component;
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit beta;
DE AltName: Full=dIII;
GN Name=pntB; Synonyms=nntB; OrderedLocusNames=Rru_A2181;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8075801; DOI=10.1099/13500872-140-7-1595;
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 and the
RT implications for the domain structure of the enzyme.";
RL Microbiology 140:1595-1604(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [3] {ECO:0007744|PDB:1PTJ}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 291-464 IN COMPLEX WITH PNTAA AND
RP SUBSTRATE ANALOG, AND CATALYTIC ACTIVITY.
RX PubMed=12791694; DOI=10.1074/jbc.m303061200;
RA Singh A., Venning J.D., Quirk P.G., van Boxel G.I., Rodrigues D.J.,
RA White S.A., Jackson J.B.;
RT "Interactions between transhydrogenase and thio-nicotinamide Analogues of
RT NAD(H) and NADP(H) underline the importance of nucleotide conformational
RT changes in coupling to proton translocation.";
RL J. Biol. Chem. 278:33208-33216(2003).
RN [4] {ECO:0007744|PDB:1U2G}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 262-464 IN COMPLEX WITH PNTAA AND
RP NADP.
RX PubMed=15323555; DOI=10.1021/bi0497594;
RA Mather O.C., Singh A., van Boxel G.I., White S.A., Jackson J.B.;
RT "Active-site conformational changes associated with hydride transfer in
RT proton-translocating transhydrogenase.";
RL Biochemistry 43:10952-10964(2004).
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|UniProtKB:P07001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
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 Evidence={ECO:0000269|PubMed:12791694};
CC -!- SUBUNIT: Complex of an alpha and a beta chain; in Rhodospirillum, the
CC alpha chain seems to be made of two subunits. {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; U05294; AAA62495.1; -; Genomic_DNA.
DR EMBL; CP000230; ABC22981.1; -; Genomic_DNA.
DR RefSeq; WP_011390030.1; NC_007643.1.
DR RefSeq; YP_427268.1; NC_007643.1.
DR PDB; 1E3T; NMR; -; A=262-464.
DR PDB; 1HZZ; X-ray; 2.50 A; C=262-464.
DR PDB; 1NM5; X-ray; 2.40 A; C=262-464.
DR PDB; 1PNO; X-ray; 2.10 A; A/B=294-464.
DR PDB; 1PNQ; X-ray; 2.40 A; A/B=294-464.
DR PDB; 1PTJ; X-ray; 2.61 A; C=291-464.
DR PDB; 1U28; X-ray; 2.30 A; C=262-464.
DR PDB; 1U2D; X-ray; 3.00 A; C=262-464.
DR PDB; 1U2G; X-ray; 2.20 A; C=262-464.
DR PDB; 1XLT; X-ray; 3.10 A; C/F/I=294-464.
DR PDBsum; 1E3T; -.
DR PDBsum; 1HZZ; -.
DR PDBsum; 1NM5; -.
DR PDBsum; 1PNO; -.
DR PDBsum; 1PNQ; -.
DR PDBsum; 1PTJ; -.
DR PDBsum; 1U28; -.
DR PDBsum; 1U2D; -.
DR PDBsum; 1U2G; -.
DR PDBsum; 1XLT; -.
DR AlphaFoldDB; Q2RSB4; -.
DR BMRB; Q2RSB4; -.
DR SMR; Q2RSB4; -.
DR STRING; 269796.Rru_A2181; -.
DR EnsemblBacteria; ABC22981; ABC22981; Rru_A2181.
DR KEGG; rru:Rru_A2181; -.
DR PATRIC; fig|269796.9.peg.2275; -.
DR eggNOG; COG1282; Bacteria.
DR HOGENOM; CLU_007866_4_0_5; -.
DR OMA; KRGMSAG; -.
DR OrthoDB; 788546at2; -.
DR PhylomeDB; Q2RSB4; -.
DR BRENDA; 1.6.1.2; 5420.
DR EvolutionaryTrace; Q2RSB4; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012136; NADH_DH_b.
DR InterPro; IPR034300; PNTB-like.
DR Pfam; PF02233; PNTB; 1.
DR PIRSF; PIRSF000204; PNTB; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..464
FT /note="NAD(P) transhydrogenase subunit beta"
FT /id="PRO_0000231665"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 316..317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12791694,
FT ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1PTJ,
FT ECO:0007744|PDB:1U2G"
FT BINDING 348..353
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12791694,
FT ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1PTJ,
FT ECO:0007744|PDB:1U2G"
FT BINDING 390..394
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12791694,
FT ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1PTJ,
FT ECO:0007744|PDB:1U2G"
FT BINDING 425..432
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12791694,
FT ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1PTJ,
FT ECO:0007744|PDB:1U2G"
FT BINDING 451..452
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12791694,
FT ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1PTJ,
FT ECO:0007744|PDB:1U2G"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1U2G"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1U28"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 418..428
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:1PNO"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:1PNO"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:1PNO"
SQ SEQUENCE 464 AA; 47808 MW; 79200D4F8861779B CRC64;
MTHSLTMAAY IVAGVLFILA LRGLSNPESA RNGNRMGMVG MAIAILTTLL SPSVQAYAWI
VLAIAIGGAI GTVIAKKVLM TALPQLVAAF HSLVGMAAVL VATGALLNPE AYGIGSAGAI
HAGSLVEMSL GLAVGAITFS GSVIAFGKLQ GLIAGKPVTF PMQHPLNAVL GILLVVLLVV
FAATESHTAY FALMILAFAL GFLLIIPIGG ADMPVVISML NSYSGWAAAG IGFTLGNPLL
IIAGALVGSS GAILSYIMCK GMNRSIFNVI LGGFGSEGGV AAAGGAAGDR SVKAGSAEDA
AFIMKNASKV IIVPGYGMAV AQAQHALREM ADVLKKEGVE VSYAIHPVAG RMPGHMNVLL
AEANVPYDEV FELEEINSSF QTADVAFVIG ANDVTNPAAK TDPSSPIYGM PILDVEKAGT
VLFIKRSMAS GYAGVENELF FRNNTMMLFG DAKKMTEQIV QAMN
