PNTB_RHORU
ID PNTB_RHORU Reviewed; 464 AA.
AC P0C188; Q59763; Q59765;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
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;
OS Rhodospirillum rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=1085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7844118; DOI=10.1007/bf00762784;
RA Yamaguchi M., Hatefi Y.;
RT "Energy-transducing nicotinamide nucleotide transhydrogenase: nucleotide
RT sequences of the genes and predicted amino acid sequences of the subunits
RT of the enzyme from Rhodospirillum rubrum.";
RL J. Bioenerg. Biomembr. 26:435-445(1994).
RN [2]
RP STRUCTURE BY NMR OF 262-464.
RX PubMed=11004437; DOI=10.1016/s0005-2728(00)00159-6;
RA Jeeves M., Smith K.J., Quirk P.G., Cotton N.P.J., Jackson J.B.;
RT "Solution structure of the NADP(H)-binding component (dIII) of proton-
RT translocating transhydrogenase from Rhodospirillum rubrum.";
RL Biochim. Biophys. Acta 1459:248-257(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 262-464.
RX PubMed=11250201; DOI=10.1016/s0969-2126(01)00571-8;
RA Cotton N.P.J., White S.A., Peake S.J., McSweeney S., Baz Jackson J.;
RT "The crystal structure of an asymmetric complex of the two nucleotide
RT binding components of proton-translocating transhydrogenase.";
RL Structure 9:165-176(2001).
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=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 -!- SUBUNIT: Complex of an alpha and a beta chain; in Rhodospirillum, the
CC alpha chain seems to be made of two subunits.
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}.
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DR EMBL; U01158; AAC43257.1; -; Genomic_DNA.
DR RefSeq; WP_011390030.1; NZ_NHSM01000143.1.
DR PDB; 2FR8; X-ray; 2.60 A; C=262-464.
DR PDB; 2FRD; X-ray; 3.20 A; C=262-464.
DR PDB; 2FSV; X-ray; 2.30 A; C=262-464.
DR PDB; 2OO5; X-ray; 2.60 A; C=291-464.
DR PDB; 2OOR; X-ray; 2.32 A; C=291-464.
DR PDBsum; 2FR8; -.
DR PDBsum; 2FRD; -.
DR PDBsum; 2FSV; -.
DR PDBsum; 2OO5; -.
DR PDBsum; 2OOR; -.
DR AlphaFoldDB; P0C188; -.
DR BMRB; P0C188; -.
DR SMR; P0C188; -.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR TCDB; 3.D.2.2.1; the proton-translocating transhydrogenase (pth) family.
DR EvolutionaryTrace; P0C188; -.
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 GO; GO:0006740; P:NADPH regeneration; NAS:ARUK-UCL.
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 Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="NAD(P) transhydrogenase subunit beta"
FT /id="PRO_0000199027"
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 HELIX 297..306
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:2FSV"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 418..428
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:2FSV"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:2FSV"
FT HELIX 452..462
FT /evidence="ECO:0007829|PDB:2FSV"
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
