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Database: UniProt
Entry: A0A428QHJ7_9HYPO
LinkDB: A0A428QHJ7_9HYPO
Original site: A0A428QHJ7_9HYPO 
ID   A0A428QHJ7_9HYPO        Unreviewed;      1105 AA.
AC   A0A428QHJ7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   ORFNames=CEP54_004563 {ECO:0000313|EMBL:RSL64766.1};
OS   Fusarium duplospermum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL64766.1, ECO:0000313|Proteomes:UP000288168};
RN   [1] {ECO:0000313|EMBL:RSL64766.1, ECO:0000313|Proteomes:UP000288168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL64766.1,
RC   ECO:0000313|Proteomes:UP000288168};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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   -!- 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:RSL64766.1}.
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DR   EMBL; NKCI01000032; RSL64766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428QHJ7; -.
DR   STRING; 1325734.A0A428QHJ7; -.
DR   Proteomes; UP000288168; 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; 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:UP000288168};
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        522..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        554..576
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        648..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        672..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        698..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        729..749
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        761..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        803..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        826..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        856..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..902
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"
SQ   SEQUENCE   1105 AA;  115186 MW;  5C5A985657ABAD41 CRC64;
     MVANMLRPLA TTAAPASASE LCASSCFVSK QLKRYKVRDA ILSRRKQWQS TFASSRQRAI
     VPAISKPLAL IRHVSVPVTP PRTYSTVVLP KTTPYDHLTV GVPTEIFPGE RRVSLTPANV
     ALLKKKGFKQ VLVERGAGTS ADFLDAAYEA AGATLVTGPK DVWSNADIIL KVRGPGLGEV
     DCMKEGQTII SLLQPAQNKE LVEKIAARKA TSFAMDMIPR ISRAQVFDAL SSMANIAGYK
     AVLEASNVFG RFLTGQVTAA GKIPPCKVLV IGAGVAGLSA IATARRMGAI VRGFDTRSAA
     REQVQSLGAE FIEVELEEDG SGAGGYAKEM SKEFIEAEMK LFKDQAKEVD IIITTALIPG
     KPAPKLLKND ILDVMKPGSV IVDLAAEAGG NCEATKKGEL AIYNDVKIIG YTDLPSRLPT
     QSSTLYSNNI TKFLLSMAPE PKAFGIDLSD EVVRGAIVTQ DGDILPPAPR PAPPPAPVKT
     EPVEAAPEPV ALTPWQKKTR EVAGVTAGMG SIIALGKWTS PLLMSNAFTF ALASLIGYRA
     VWGVAPALHS PLMSVTNAIS GMVGIGGLFI LGGGFLPETV PQAFGALSVL LAFVNVGGGF
     VITKRMLDMF KRPTDPPEYP WLYAIPAALC GGGFVAAAST GAAGLVQAGY LISSVLCIGS
     ISSLASQATA RMGNMIGILG VGTGVLASLL AAGFTPEVLT QFGGLAALGT IAGFLIGKRI
     TPTDLPQTVA ALHSVVGLAA VLTSIGSVMA DVMDPSTLHL VTAYLGVLIG GITFTGSIVA
     FLKLGGRMSS KPKILPGRHA INSGLLATNV ATMGAFVTMA PGSPMIAAGA LAANAALSFI
     KGYTTTAAIG GADMPVVITV LNAYSGFALV AEGFMLDNPL LTTVGALIGV SGSILSYIMC
     VAMNRSLTNV LFGGLGTPTA MQEYKPQGEV TTTSVEDLAD ALLNSEKVIL IVGYGMAVAK
     AQYALSSIVS SLRAKGITVR FAIHPVAGRM PGQCNVLLAE ASVPYDIVLE MDEINDDFPD
     TDLAVVIGAN DTVNPIALEK GSSIEGMPVL HAWKAKQVVV MKRSLASGYA DVPNPMFYMP
     NAKMLFGDAR VTCEAIKSAI ESKSS
//
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