ID G3JU79_CORMM Unreviewed; 1112 AA.
AC G3JU79;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=CCM_09408 {ECO:0000313|EMBL:EGX87786.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX87786.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX87786.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX87786.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126407; EGX87786.1; -; Genomic_DNA.
DR RefSeq; XP_006674605.1; XM_006674542.1.
DR AlphaFoldDB; G3JU79; -.
DR STRING; 983644.G3JU79; -.
DR GeneID; 18171411; -.
DR KEGG; cmt:CCM_09408; -.
DR VEuPathDB; FungiDB:CCM_09408; -.
DR eggNOG; ENOG502QQ0A; Eukaryota.
DR HOGENOM; CLU_003376_0_0_1; -.
DR InParanoid; G3JU79; -.
DR OMA; KLFMEQC; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
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 Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
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; PS00836; ALADH_PNT_1; 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:UP000001610};
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 530..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..244
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 253..417
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1112 AA; 115264 MW; 14B5898E422AC98B CRC64;
MASHFLRPLA CELSSSSSAA PARLARISFQ DGRLLVSSSS SSRRRRWLTT LNKASSTASS
SVPAAAAATP LALARRHAAV VALLPPPPKR YSTVVLPQTT PYAQLTVGVP TETFAGERRV
AVTPANVAVL LKKGYAKVLV QRGAGTAADF LDSAYEKAGA TLVADAAAIW SQAHIVLKVR
GPSLDEVDAI RDHQTIISLL QPAQNKALVE KIASRHATCL AMDMIPRISR AQVFDALSSM
ANIAGYKAVL EASNVFGRFL TGQVTAAGKI PPCKVLVIGA GVAGLSAIAT ARRMGAIVRG
FDTRPAAREQ VQSLGAEFIE VEIDEDGSGA GGYAKEMSKE FIDAEMKLFK EQAKDVDIII
TTALIPGKPA PKLLKMDMLD VMKPGSVIVD LAAEAGGNCE ATKPGELAVY NDVKVIGYTD
LPSRLPTQSS TLYSNNITKF LLSMAPQEQA FGIDLSDEVV RGAIVTLKGD IIPPAPRPAP
PPPAAKPAAA AEAVPEPVAL TPWQVKSREV GFVTGGMASV LALGKFTSPL FMSNAFTFAL
ASLIGYRVIW GVAPALHSPL MSVTNAISGM VGVGGLFILG GGYLPGTIPQ TLGALSVLLA
FVNVGGGFVI TKRMLDMFKR PTDPPEYPWL YAVPAAVFGG GFVAAAATGV GGLVQAGYLA
SSVLCIGSLS SLASQSTARM GNMLGMLGVS SGVLASLLAA GFSPEVLTQF GALASIGILA
GALIGKRITP TDLPQTVAAL HSVVGLAAVL TSIGSVMAGI QDISTLHMVT GYLGVLIGGI
TFTGSIVAFL KLGGRMSSKP KILPGRHFIN GGLLAGNMAT MGAFITMAPG APLIAAGALT
ANAVMSFIKG YTTTAAIGGA DMPVVITVLN AYSGFALVAE GFMLDNSLLT TVGALIGVSG
SILSYVMCVA MNRSLTNVLF GGLSAPAAEA QEYQPQGEVT KTSSDELADA LLNSESVILV
VGYGMAVAKA QYAISEIVAL LRAKGITVRF AIHPVAGRMP GQCNVLLAEA SVPYDIVLEM
DEINDDFPDT DLTVVIGAND TVNPIAMEKG SAIEGMPVLH AWKSKQVVVM KRGMASGYAD
VPNPMFYMPN TKMLFGDAKD TCEAIKTALQ SK
//