ID V9WJ71_9RHOB Unreviewed; 477 AA.
AC V9WJ71;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=Gal_02488 {ECO:0000313|EMBL:AHD10233.1};
OS Phaeobacter gallaeciensis DSM 26640.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD10233.1, ECO:0000313|Proteomes:UP000018782};
RN [1] {ECO:0000313|EMBL:AHD10233.1, ECO:0000313|Proteomes:UP000018782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD10233.1,
RC ECO:0000313|Proteomes:UP000018782};
RA Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT 105210T.";
RL Submitted (DEC-2013) 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; CP006966; AHD10233.1; -; Genomic_DNA.
DR RefSeq; WP_024097875.1; NZ_AOQA01000007.1.
DR AlphaFoldDB; V9WJ71; -.
DR GeneID; 31846861; -.
DR KEGG; pgd:Gal_02488; -.
DR PATRIC; fig|1423144.3.peg.2483; -.
DR eggNOG; COG1282; Bacteria.
DR HOGENOM; CLU_007866_4_0_5; -.
DR OrthoDB; 9763786at2; -.
DR Proteomes; UP000018782; 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:AHD10233.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018782};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..473
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 477 AA; 49837 MW; BAB687F31E0B7FA8 CRC64;
MDFGFTTAAY VVAAVLFILS LGGLSGQESA KRAVWYGIAG MALAVLATLI GPGAGLWLLS
IVLIAAGGLI GYYVAKRVQM TEMPQLVAAM HSLVGLAAVF VGFIAHIELG RVLAMDDTVK
KALEGFGALL AKKDGVEIAI LRGELFLGVF IGAVTFTGSV IAYGKLAGKV SSAATKLPGG
HMLNAGAAGL SLICLIWYFN TGGFFPLFLM TLAALFIGYH LIMGIGGADM PVVVSMLNSY
SGWAAAAIGF SLGNDLLIVV GALVGSSGAI LSYIMCKAMN RSFISVILGG FGGTAGPAME
IDGEQIAIEA DGVATALDEA DSVVIIPGYG MAVAQAQQNV AELTRRLRAK GKNVRFAIHP
VAGRLPGHMN VLLAEAKVPY DIVLEMDEIN EDFPETDVAI VIGSNDIVNP AAQEDPNSPI
AGMPVLECWK AKQVFVSKRG QGTGYSGIEN PLFFKENTRM FYGDAKASLD KLLTMIS
//
