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Database: UniProt
Entry: A0A0R0MAG2_9BURK
LinkDB: A0A0R0MAG2_9BURK
Original site: A0A0R0MAG2_9BURK 
ID   A0A0R0MAG2_9BURK        Unreviewed;       471 AA.
AC   A0A0R0MAG2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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:KRH98726.1};
GN   ORFNames=AO057_04340 {ECO:0000313|EMBL:KRH98726.1};
OS   Curvibacter sp. PAE-UM.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Curvibacter.
OX   NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRH98726.1, ECO:0000313|Proteomes:UP000051912};
RN   [1] {ECO:0000313|EMBL:KRH98726.1, ECO:0000313|Proteomes:UP000051912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAE-UM {ECO:0000313|EMBL:KRH98726.1,
RC   ECO:0000313|Proteomes:UP000051912};
RA   Ma D.;
RT   "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT   river sediment.";
RL   Submitted (SEP-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}.
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:KRH98726.1}.
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DR   EMBL; LKCX01000031; KRH98726.1; -; Genomic_DNA.
DR   RefSeq; WP_057674480.1; NZ_KQ483358.1.
DR   AlphaFoldDB; A0A0R0MAG2; -.
DR   STRING; 1714344.AO057_04340; -.
DR   OrthoDB; 9763786at2; -.
DR   Proteomes; UP000051912; 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   Oxidoreductase {ECO:0000313|EMBL:KRH98726.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051912};
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..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..466
FT                   /note="NADP transhydrogenase beta-like"
FT                   /evidence="ECO:0000259|Pfam:PF02233"
SQ   SEQUENCE   471 AA;  49278 MW;  7296F65A3684994F CRC64;
     MSQSLATVAY LGAAILFILS LGGLSNPETS RRGNLFGMVG MALAVLATVF GPRVSAAGIP
     WIIAALVLGG SIGLYAARVV KMTQMPELVA LMHSLVGLAA CLVGFASYVD TSIQLAGAEK
     VIHEVEIYIG ILIGAVTFSG SLIAFGKLNG KIGGKPLLLP ARHWLNLAGL LIVIWFGREF
     IQAKTVAEGM TPLIVMTVIA LLFGIHMVMA IGGADMPVVV SMLNSYSGWA AAATGFMLSN
     DLLIVTGALV GSSGAILSYI MCNAMNRNFI SVIAGGFGSG GGSTPAKSGE AAQPQGEVVP
     VNAADTAELL RDAKSVIIVP GYGMAVAQAQ HTVYEITRTL REKGVKVRFA IHPVAGRMPG
     HMNVLLAEAK VPYDIVMEMD EINEDFPGTD VAMVIGANDI VNPAAQDDPA SPIAGMPVLE
     VWKAKTSIVM KRSMASGYAG VDNPLFYKEN NRMLFGDAKK MLDEVLGALK A
//
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