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Database: UniProt
Entry: Q5GWN8_XANOR
LinkDB: Q5GWN8_XANOR
Original site: Q5GWN8_XANOR 
ID   Q5GWN8_XANOR            Unreviewed;       495 AA.
AC   Q5GWN8;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
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:AAW76883.1};
GN   OrderedLocusNames=XOO3629 {ECO:0000313|EMBL:AAW76883.1};
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW76883.1, ECO:0000313|Proteomes:UP000006735};
RN   [1] {ECO:0000313|EMBL:AAW76883.1, ECO:0000313|Proteomes:UP000006735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA   Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA   Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW76883.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5GWN8; -.
DR   STRING; 291331.XOO3629; -.
DR   KEGG; xoo:XOO3629; -.
DR   HOGENOM; CLU_007866_4_0_6; -.
DR   Proteomes; UP000006735; 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   Reference proteome {ECO:0000313|Proteomes:UP000006735};
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        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..442
FT                   /note="NADP transhydrogenase beta-like"
FT                   /evidence="ECO:0000259|Pfam:PF02233"
SQ   SEQUENCE   495 AA;  51785 MW;  5F3CA89B55519313 CRC64;
     MNLSTAELLS WFVKTSYLVA ATLFLPELHN VPLILAALAI GTGVAWWSAK KVAITDMPQM
     VALYNGMGGG SAAAIGAVEL LRFSFFANCD TAHWSAQAIA ELAARRPDTT AVAVAVIGSA
     IGAVSLSGSI IAWAKLDGRL DRRVTFPGQQ VFNLVVAVAV LVLGIWAASS LQPLAIIAFF
     VAALALGVLM TLPIGGADMP VVISLYNAFT GLAVAFEGYV LGNEALIIAG MMVGAAGILL
     TRLMAKAMNR PISGVLFSNF GGGGQAQEIS GTQKPIEAGD VAAMMAFAER VVIVPGYGMA
     VAQAQHKIWE LAQRLIARGA KVKFAIHPVA GRMPGHMNVL LAEAGVPYDL IADMDDINPE
     FASTDVSLVI GANDVVNPVA KTDPASPIYG MPILDVVNSR NTVVIKRGKG TGFAGIENAL
     FYADNTRMLY GDGAEAAGAL VSELKALDGG GLECWCVARC AQMLRTCSRS PEQQCQERQM
     DELQAGIEPS LAVLP
//
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