ID A0A0D2CH45_9EURO Unreviewed; 1108 AA.
AC A0A0D2CH45;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-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=PV07_11152 {ECO:0000313|EMBL:KIW22904.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW22904.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW22904.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW22904.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847046; KIW22904.1; -; Genomic_DNA.
DR RefSeq; XP_016243120.1; XM_016398558.1.
DR AlphaFoldDB; A0A0D2CH45; -.
DR STRING; 569365.A0A0D2CH45; -.
DR GeneID; 27350346; -.
DR VEuPathDB; FungiDB:PV07_11152; -.
DR HOGENOM; CLU_003376_0_0_1; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000054466; 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; IPR008143; Ala_DH/PNT_CS2.
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.
DR PROSITE; PS00837; ALADH_PNT_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000054466};
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 521..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..237
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 246..410
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 463..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 116327 MW; 54C3CA5F69DB18BA CRC64;
MAHASFPVLS APLSVKLSTK SCFSFRDSVP ALGAIYGCVR QRRHAKRHVH SLSCGLVPLT
SINQHQHKSL IKLPPRAVAV WSRFKSDLPA EPVLYSQLTI GVPKETHPGE RRVAVAPQNI
PLLLKKGFAR VLVERGAGIE AEYADEVYEH VGATVVDRET VWSESNILLK VRPPNLESEV
PNIREGTALI SFLQPMQNRP LVEALASQRV TAFAMDMIPR ISRAQAFDAL SSMANIAGYK
AVLEASNHYG RFLTGQVTAA GKIPPSKVLV IGAGVAGLSA ITTARRLGAI VRGFDTRSAA
REQVQSLGAD FLEVSVKEEG SAAGGYSKEM SKEFIEAEMK LFMEQCKEVD IVVTTAAIPG
RPSPKLITEK MVSAMKPGSV IVDLASEGGG NCEVTQPGKL IVHNHVTIIG YTDFPSRLPT
QSTSLYSNNI TKFLLAISPK DNHFGIDLED EVVRGSIVTH DGKIIPPAPR PAPPPAPVQQ
HHEHESKPVE LTPWQSQARN AAAVTGGMSA ALALGKLTSP LFMGSAFTAG LAGLIGYRSV
WGVIPALHSP LMSVTNAISG IVGVGGFFIM GGGYLPETVP QALGALSVLL AFVNVSGGFV
ITKRMLDMFK RPTDPPEYPW LYAIPGVLFA GGFIAAASTG MAGLVQAGYL VSSLLCIGSI
QGLASQATAR TGNLLGILGV LAGIIASLGA VGFSPEVLTQ FGAIATIGGI VGALIGRRIT
PTELPQTVAA LHSVVGLAAV LTSIGSVLAD VSDISTLHMV TAYLGVLIGG VTFTGSLVAF
LKLAGRMSSR PTILPGRHII NSSLLAANAG TMGAFLTMAP GAPAVAAVCL SANTALSFAK
GFTTTAAIGG ADMPVVITVL NAYSGFALVA EGFMLDNPLL LTVGSLIGVS GSILSYIMCV
AMNRSLTNVL FGGIAPIAQT SHEIKGQITK TTVEETVEAL ANAESVIIVV GYGMAVAKAQ
YAIAEIVSLL RSKGVNVRFA IHPVAGRMPG QCNVLLAEAS VPYDIVLEMD EINDDFPETD
LTLVIGANDT VNPIALEPGS PIAGMPVLHA WKSKGVVVMK RGMSSGYADV PNPMFYMPGT
RMLFGDAKQT CDALKAALET RYKAQFHV
//
