ID W9C0H7_9SPHN Unreviewed; 502 AA.
AC W9C0H7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|ARBA:ARBA00014581, ECO:0000256|PIRNR:PIRNR000204};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943, ECO:0000256|PIRNR:PIRNR000204};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
GN ORFNames=Q27BB25_02050 {ECO:0000313|EMBL:ESZ88914.1};
OS Blastomonas sp. CACIA14H2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Blastomonas.
OX NCBI_TaxID=1419876 {ECO:0000313|EMBL:ESZ88914.1, ECO:0000313|Proteomes:UP000019523};
RN [1] {ECO:0000313|EMBL:ESZ88914.1, ECO:0000313|Proteomes:UP000019523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIA14H2 {ECO:0000313|Proteomes:UP000019523};
RX PubMed=24435876;
RA Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Lima C.P.,
RA Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT "Draft Genome Sequence of Blastomonas sp. Strain CACIA 14H2, a
RT Heterotrophic Bacterium Associated with Cyanobacteria.";
RL Genome Announc. 2:e01200-13(2014).
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:0000256|ARBA:ARBA00003943,
CC ECO:0000256|PIRNR:PIRNR000204}.
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:0000256|ARBA:ARBA00000006,
CC ECO:0000256|PIRNR:PIRNR000204};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PNT beta subunit family.
CC {ECO:0000256|ARBA:ARBA00007919, ECO:0000256|PIRNR:PIRNR000204}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESZ88914.1}.
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; AYSC01000002; ESZ88914.1; -; Genomic_DNA.
DR AlphaFoldDB; W9C0H7; -.
DR STRING; 1419876.Q27BB25_02050; -.
DR PATRIC; fig|1419876.3.peg.407; -.
DR Proteomes; UP000019523; Unassembled WGS sequence.
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 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 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 {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000204};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR000204};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000204};
KW NAD {ECO:0000256|PIRNR:PIRNR000204};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000204};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000204};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..502
FT /note="NAD(P) transhydrogenase subunit beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004917973"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..498
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 502 AA; 52279 MW; 68ABE5499564F7BD CRC64;
MNINRPLTFA AAACSALTAA PAFASGGDAA PVSPWVSLAY LVAGVFFILA LRGLSSPETS
RSGNRFGMIG MAIAVITTLL THEIANIVEI LIAIAIGGVA GFVIARKIKM TDMPQLVAAF
HSLVGLAAVL VALAAWLNPE AFGILDANGQ ILTVSRIEMG LGVAIGAITF SGSVIAFLKL
NGNMSGSPIM LPGRHVINLG VLAAILGMIA VYTVSPDGGA GEGWLFLAIT VLSFIIGFLL
IIPIGGADMP VVVSMLNSYS GWAAAAMGFT LSNTAMIITG ALVGSSGAIL SYIMCKAMNR
SFISVIAGGF GAEASSGGDG AAKVDRPWKR GSAEDAAYMM KQAESVIIVP GYGMAVAQAQ
HALREMADLL KKEGVSVKYA IHPVAGRMPG HMNVLLAEAN VPYDEVFELE DINSEFSQTD
VAFIIGANDV VNPAAKTDKS SPIYGMPVFD VDKAKTVFFI KRSMGGVGYA GVDNDVFYMD
QTMMLLADAK KMVEDIVKNL GH
//
