ID F4LX66_TEPAE Unreviewed; 464 AA.
AC F4LX66; L0S2K5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntB {ECO:0000313|EMBL:CCP26674.1};
GN OrderedLocusNames=TEPIRE1_1871 {ECO:0000313|EMBL:CCP26674.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP26674.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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};
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DR EMBL; HF563609; CCP26674.1; -; Genomic_DNA.
DR RefSeq; WP_013778787.1; NC_019954.2.
DR AlphaFoldDB; F4LX66; -.
DR STRING; 1209989.TepRe1_1732; -.
DR KEGG; tae:TepiRe1_1871; -.
DR KEGG; tep:TepRe1_1732; -.
DR PATRIC; fig|1209989.3.peg.2155; -.
DR eggNOG; COG1282; Bacteria.
DR HOGENOM; CLU_007866_4_0_9; -.
DR OrthoDB; 9763786at2; -.
DR Proteomes; UP000010802; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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 SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000313|EMBL:CCP26674.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..460
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 464 AA; 48855 MW; 26FAD41AA3BD33DE CRC64;
MIGTYEIVSI VLSILVLVGI KLMSSPKTAV QGNRIGAMAM LAAVIVVLAY NGIIDVPLLW
FAIFVGGVTG YIMAMRVKMI QMPQMVALLN GLGGGASALV ALVEIFERYK QMTLFGRLTG
QLALAVGAVT FSGSLIAAAK LDRRISQRPI ILKNHGLISN AVLLIIILLI ITASVANISG
IGFIAIITAF LALAYGVLFA IRVGGADMPI TISLLNSFSG LAGAICGFTI EDPLLVAVGA
IVGASGLILT QIMCGAMNRS LVDILSGSQL NSGINKKETT PKEKVIDVGK PPVTAKKLPA
EILKTAKKVV IVPGYGMAIA QAQSQVKALY DTLESQGKEV KFAIHPVAGR MPGHMNVLLA
EVDVPYDKLC EMDVINPEFS ETDVAIVVGA CDVINPAANT AEGTPIYGMP VLKVEEAKNV
IVCNLDTKPG YSGVENSLYE LLHVHLLLGN AADTVKELVE VIKQ
//
