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Database: UniProt
Entry: A0A0P0MI16_9BURK
LinkDB: A0A0P0MI16_9BURK
Original site: A0A0P0MI16_9BURK 
ID   A0A0P0MI16_9BURK        Unreviewed;       473 AA.
AC   A0A0P0MI16;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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   Name=pntB {ECO:0000313|EMBL:ALK92786.1};
GN   ORFNames=L103DPR2_02404 {ECO:0000313|EMBL:ALK92786.1};
OS   Limnohabitans sp. 103DPR2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK92786.1, ECO:0000313|Proteomes:UP000063254};
RN   [1] {ECO:0000313|EMBL:ALK92786.1, ECO:0000313|Proteomes:UP000063254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103DPR2 {ECO:0000313|EMBL:ALK92786.1,
RC   ECO:0000313|Proteomes:UP000063254};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP011834; ALK92786.1; -; Genomic_DNA.
DR   RefSeq; WP_055361290.1; NZ_CP011834.1.
DR   AlphaFoldDB; A0A0P0MI16; -.
DR   STRING; 1678129.L103DPR2_02404; -.
DR   KEGG; lim:L103DPR2_02404; -.
DR   PATRIC; fig|1678129.3.peg.2385; -.
DR   OrthoDB; 9763786at2; -.
DR   Proteomes; UP000063254; Chromosome.
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   Oxidoreductase {ECO:0000313|EMBL:ALK92786.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063254};
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   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..468
FT                   /note="NADP transhydrogenase beta-like"
FT                   /evidence="ECO:0000259|Pfam:PF02233"
SQ   SEQUENCE   473 AA;  49614 MW;  3D60B0E988DF5121 CRC64;
     MTSNLSTVAY IGATILFILS LGGLSNQETA RRGNLYGMVG MTLAVLATVL GPQVTSAGTP
     WIVGSLVIGG AIGLYAARAV QMTQMPELVA LMHSMVGMAA VLVGYATFVD PEATKGFEGA
     AHTIHAMEIY IGIFIGAVTF SGSVAAFGKL SGRIGGSPLL LPARHWINLA GLLAVVYFGR
     LFLQAETIEQ GMMPLFVMSA IALLFGIHMV MAIGGADMPV VVSMLNSYSG WAAAATGFML
     NNDLLIVVGA LVGSSGAILS YIMCNAMNRS FISVIAGGFG TTAAAPKPAE GASAEPQGEV
     SPILAAETAE LLRDAKNVII VPGYGMAVAQ AQHTVFEITR TLREKGVNVR FGIHPVAGRM
     PGHMNVLLAE AKVPYDIVLE MDELNEDFPD TDVAIVIGAN DIVNPAAQDD PASPIAGMPV
     LEVWKARTSI VMKRSMASGY AGVDNPLFYK DNNRMLFGDA KKMLDEVLVS LKS
//
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