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Database: UniProt
Entry: H0R3C5_9ACTN
LinkDB: H0R3C5_9ACTN
Original site: H0R3C5_9ACTN 
ID   H0R3C5_9ACTN            Unreviewed;       502 AA.
AC   H0R3C5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:GAB19576.1};
GN   ORFNames=GOEFS_092_00010 {ECO:0000313|EMBL:GAB19576.1};
OS   Gordonia effusa NBRC 100432.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB19576.1, ECO:0000313|Proteomes:UP000035034};
RN   [1] {ECO:0000313|EMBL:GAB19576.1, ECO:0000313|Proteomes:UP000035034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB19576.1,
RC   ECO:0000313|Proteomes:UP000035034};
RA   Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL   Submitted (DEC-2011) 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:GAB19576.1}.
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DR   EMBL; BAEH01000092; GAB19576.1; -; Genomic_DNA.
DR   RefSeq; WP_007318911.1; NZ_BAEH01000092.1.
DR   AlphaFoldDB; H0R3C5; -.
DR   STRING; 1077974.GOEFS_092_00010; -.
DR   eggNOG; COG1282; Bacteria.
DR   OrthoDB; 9763786at2; -.
DR   Proteomes; UP000035034; 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   Reference proteome {ECO:0000313|Proteomes:UP000035034};
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        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..497
FT                   /note="NADP transhydrogenase beta-like"
FT                   /evidence="ECO:0000259|Pfam:PF02233"
SQ   SEQUENCE   502 AA;  51144 MW;  79E3ACF41E7CD4C8 CRC64;
     MSSSVLSASE GAVVSEALGY GVTVLYIVAF SLFIYGLMGL TGPKTAVRGN WIAAVGMGIA
     IVATLLGVYN SAGDAGVPGI NWILIVAGLL VGVVLGIPPA LKTKMTAMPQ LVALFNGVGG
     GTVALIAWAE YIEYRGFTTV PDTPDVHVIV GSLFAAIIGS VSFWGSLVAF AKLQELLNKN
     LEKKLVAGAK AFQLANIVLA LVAIGIAIYI GIKAGAGDGP TPWFWIVGLL VAAGLMGLFV
     VFPIGGADMP VVISLLNAMT GLSAAAAGLA LNNQAMIVAG MIVGASGSIL TNLMAKAMNR
     SIPAIIFGSF GGGDDGAAGA PGATGGTVKA TSAADAAIQM AYANQVIVVP GYGLAVAQAQ
     HAVKEMAALL EAKGVEVKYA IHPVAGRMPG HMNVLLAEAD VEYDAMKEMD DINGEFGRTD
     VAIVIGANDV TNPAARNDPS SPIHGMPILN VDQARSTIVL KRSMSSGYAG IENPLFFADG
     TSMLFGDAKK SVGSVIEELK AL
//
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