ID A0A0V1HW64_9BILA Unreviewed; 1079 AA.
AC A0A0V1HW64;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=NNT {ECO:0000313|EMBL:KRZ15016.1};
GN ORFNames=T11_9820 {ECO:0000313|EMBL:KRZ15016.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ15016.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ15016.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ15016.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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:KRZ15016.1}.
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DR EMBL; JYDP01000020; KRZ15016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HW64; -.
DR STRING; 268475.A0A0V1HW64; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR InterPro; IPR034300; PNTB-like.
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; PF02233; PNTB; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000055024};
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 475..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 716..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 759..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..190
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 199..364
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1079 AA; 115335 MW; C824778F3F88AEDA CRC64;
MVLLKLCHDE VISYVRLFQV IRLHKQNFTK SAYLKEQVQT GDKVQIKNGI LYSELSIGVP
KEISKEQRVA VTPNVAQTLV KKGFQVNMEK DAGLLAKFSN DDYLNVGAKI ASKEEAFGSD
IVLKVRAPLE NEVEKFKSNS TLISFLYPAQ NENILKLLAK KKLTVFAMDC IPRISRAQVF
DALSSMANIA GYKAVIEAAN HFGRFFTGQI TAAGKVPPAK VLVIGGGVAG LAAIGTAKNM
GAIVRGFDTR SAVKEQVQSL GAEFLEINIK ESGEGVGGYA KEMSKEYIEA EMQLFAKQCK
DIDILITTAL IPGKPAPKLF TKQMIQSMKP GSVVVDLASE AGGNVETTHP GELYVSDNGV
VHIGYTDFPS RLPTTASMLY ANNISKFLLS LGDKEHFFVD LNDDVTRGAI ILDKGSMMWP
PPKIEDPSPA VQQPKVEVKE LPKEPNYFME TLKNAGLYTS GFGSIVGLGF IAPNAAFSTM
CTTFGLAGIV GYHTVWGVTP ALHSPLMSVT NAISGITAAG GLLLMGGNYL PSTIPQSLAA
LACFISSINI GGGFLITQRM LDMFKRPTDP PEYNYLYLMP AAVFLGGYGY GFYGNYNEIH
SLCYLGSSLA CVGALAGLSS QKTCRLGNAL GMIGVAGALV STIGNLNPSQ QLLAQMLSCM
GVGGAIGLGI AKRIEVTSLP QLVAAFHSFV GVAAMLTCVA NFMVDHEHFI IDPSLAVNKC
ALFLGTFIGG VTFTGSLMAF GKLQGILNSA AVLLPGRHAL NTALTLGNVA ALIMYMNTHD
YSTGLNMLAS TATLSSIMGV TMTMAIGGAD MPVVITVLNS YSGWALCAEG FMMNNQLLTI
VGALIGSSGA ILSYIIIKKE FEYPCFKAMN RSLTNVILGG FGTSSTGAGK PKEITGTHTE
VDVDQVGVFK TVDWLLNAKN VIIVPGYGLC AAHAQYPIAE MVTLLRNHNI NVRFGIHPVA
GRMPGQLNVL LAEAGVPYDI VLEMDEINDD FPSTDLVLVI GANDTVNSAA EDDPNSIIAG
MPVLRVWKAN QVVVMKRSLG VGYAAVDNPI FYNENTAMLL GDAKKTCDNL LEKLKKKME
//
