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Database: UniProt
Entry: D7H678_BRUAO
LinkDB: D7H678_BRUAO
Original site: D7H678_BRUAO 
ID   D7H678_BRUAO            Unreviewed;       466 AA.
AC   D7H678;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=BAYG_01999 {ECO:0000313|EMBL:EFH32488.1};
OS   Brucella abortus bv. 5 str. B3196.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH32488.1, ECO:0000313|Proteomes:UP000005752};
RN   [1] {ECO:0000313|EMBL:EFH32488.1, ECO:0000313|Proteomes:UP000005752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3196 {ECO:0000313|EMBL:EFH32488.1,
RC   ECO:0000313|Proteomes:UP000005752};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Brucella abortus bv. 5 str. B3196.";
RL   Submitted (FEB-2010) 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; GG774528; EFH32488.1; -; Genomic_DNA.
DR   RefSeq; WP_002965677.1; NZ_GG774528.1.
DR   AlphaFoldDB; D7H678; -.
DR   GeneID; 58777213; -.
DR   HOGENOM; CLU_007866_4_0_5; -.
DR   Proteomes; UP000005752; 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   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..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..462
FT                   /note="NADP transhydrogenase beta-like"
FT                   /evidence="ECO:0000259|Pfam:PF02233"
SQ   SEQUENCE   466 AA;  48509 MW;  B629260EDDE613EC CRC64;
     MSVNLAAFLY LVSGVLFILA LRGLSHPTTS RQGNMYGMIG MAISIVTTLL LARPSFGGLV
     LIIVGIAIGG GIGAVIARRI AMTAMPQLVA AFHSLIGLAA VLVAAAALYS PHSFGIGEVG
     QIHGQALIEM SLGVAIGAIT FTGSIIAFLK LDGRMSGKPI MLPGRHVINA ALAAAIVLLI
     VVLTNTESHF VFWLIVLLSL VFGVLIIVPI GGADMPVVVS MLNSYSGWAA AGIGFTLGNL
     ALIITGALVG SSGAILSYIM CKGMNRSFIS VILGGFGGDT SSAAGGEVEQ RPVKQGSADD
     AAFILKNASK VIIVPGYGMA VAQAQHALRE MADKLKAEGV EVKYAIHPVA GRMPGHMNVL
     LAEANVPYDE VFELEDINSE FATADVAFVI GANDVTNPAA KTDPKSPIFG MPILDVDKAG
     TVLFIKRGMG SGYAGVENEL FFRDNTMMLF ADAKKMVESI VKALDH
//
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