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Database: UniProt
Entry: G3JU79_CORMM
LinkDB: G3JU79_CORMM
Original site: G3JU79_CORMM 
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
//
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