ID A0A099CTT2_9GAMM Unreviewed; 473 AA.
AC A0A099CTT2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=HNQ86_002975 {ECO:0000313|EMBL:MBB6185630.1}, LF63_0111350
GN {ECO:0000313|EMBL:KGI77199.1};
OS Oleiagrimonas soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Oleiagrimonas.
OX NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI77199.1, ECO:0000313|Proteomes:UP000029708};
RN [1] {ECO:0000313|EMBL:KGI77199.1, ECO:0000313|Proteomes:UP000029708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.5X {ECO:0000313|EMBL:KGI77199.1,
RC ECO:0000313|Proteomes:UP000029708};
RA Fang T., Wang H.;
RT "Xanthomonadaceae 3.5X direct submission.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6185630.1, ECO:0000313|Proteomes:UP000560000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 107085 {ECO:0000313|EMBL:MBB6185630.1,
RC ECO:0000313|Proteomes:UP000560000};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:KGI77199.1}.
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DR EMBL; JROI01000013; KGI77199.1; -; Genomic_DNA.
DR EMBL; JACHET010000001; MBB6185630.1; -; Genomic_DNA.
DR RefSeq; WP_043101905.1; NZ_KN196470.1.
DR AlphaFoldDB; A0A099CTT2; -.
DR STRING; 1543381.LF63_0111350; -.
DR HOGENOM; CLU_007866_4_0_6; -.
DR OrthoDB; 9763786at2; -.
DR Proteomes; UP000029708; Unassembled WGS sequence.
DR Proteomes; UP000560000; 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:MBB6185630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029708};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..466
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 473 AA; 49145 MW; B02588E08C4E6601 CRC64;
MHADVLTRWL PEAIRACYLI AALLFILGLK RMSSPRTARG GVVWAGVGML LAVLATLLLP
GMHHLGLIVL GIAVAGGLAW WSGKRVAMTD MPQMVALYNG MGGGAAAAIG VFELVGAARV
AAMGGVDAMA PAALVLAVLG VLIGAVSFSG SLIAFAKLQG WMDRRFVFPG QQVFNVLILL
LAVVLGGVLI FAPPAMAVIA GFLLAALAFG LLMTLPIGGA DMPVVISLYN ALTGLAVAFE
GFVLQNEAMI IAGTVVGAAG TLLTQLMAKA MNRSLGNVLF GSFGAAAGEA QAIDGAQKEI
EAPDAAVMMA YAERVVIVPG YGMAVAQAQH KIWEFAHQLI ERGVKVRFAI HPVAGRMPGH
MNVLLAEAGV PYDLIVDMED VNPEFPNTDV VLVIGANDVV NPVAKTDPAS PIYGMPVLDV
VAAKQAIVIK RGRGKGFAGI ENALFYADNT RMLFGDGQAM AAQLVSELKS LDA
//
