ID A0A0N9NJZ2_9ACTN Unreviewed; 509 AA.
AC A0A0N9NJZ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=ACH46_19770 {ECO:0000313|EMBL:ALG86313.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG86313.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG86313.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG86313.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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 -!- 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 -!- 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}.
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DR EMBL; CP011853; ALG86313.1; -; Genomic_DNA.
DR RefSeq; WP_062394502.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N9NJZ2; -.
DR STRING; 1136941.ACH46_19770; -.
DR KEGG; goq:ACH46_19770; -.
DR PATRIC; fig|1136941.3.peg.4047; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000063789; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR NCBIfam; TIGR00561; pntA; 1.
DR PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 400..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 146..310
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 509 AA; 52729 MW; 257DB12755592C30 CRC64;
MLIGIPRESK AGETLVAATG KTVAQLQTLG YDVIVQAGAG ELAEQPDKAF SDAGTRIGTV
EEVWGADIVV KVNAPTDEEI ARLRRGAVLI SMMAPGRNPE LLEKLQNAGV TALAMDAVPR
ISRAQSMDVL SSMANVAGYR AVVEAAHEFG RMFTGQVTAA GKIPPARVFV VGAGVAGLAA
IGAASAMGAV VRAFDVRPEV AEQVQSMGAE FVQVDFEAEK SEDGYAKEMT AEQEAATASM
YDEEARGADI VITTAQIPGR PAPRLISAET VAAMKHGSVI VDMAASSGGN AAGAVADEKV
VTENGVTILG YTDLAGRLAA QTSQLYGTNI VNLLKLLTPE KNGELTLDMD DIVQRGITVT
RDGEGMWPPP PVQVSAAPKA AAVEVPVAEP KEPMSPAKKV GLALIGIILF GVVVAFAPAP
LPEHFTVLML AIVIGYYVIG NVAHALHTPL MSVTNAISGV VIVGALLQLA TNNVTVMVLA
TIAILVASIN VFGGFAVTRR MLAMFSKGA
//