ID A0A0F4GQB6_9PEZI Unreviewed; 1094 AA.
AC A0A0F4GQB6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=TI39_contig367g00005 {ECO:0000313|EMBL:KJX99247.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX99247.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX99247.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX99247.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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 -!- 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:KJX99247.1}.
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DR EMBL; LAFY01000359; KJX99247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GQB6; -.
DR STRING; 1047168.A0A0F4GQB6; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000033647; 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; 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:UP000033647};
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 509..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 569..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 716..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 813..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..225
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 234..398
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 114219 MW; D8A8259713B973E8 CRC64;
MWPACRPLRP YCSSAKTSLP HILGALTQTR LLYSSPKWRQ EASADTAGQA ASFTPPPPDS
ITPPAKEEVK AIPYSELTIG VPLEVRTGEK RVAITPQNAA LLLKKGFKAV LVEHGAGFQA
QFPAHDYEAA GATLVNASRV WYDSNIVLKV RPPRLRSTTL SPNNFIQGFR EGGVLISILQ
PNIDKNKKII DVMAEKKLTS FAMDMIPRIT RAQSFDVLSS MANIAGYKAV LEASNHFGRY
LTGQTTAAGK VPPCKVLVIG AGVAGLSAIA TARRMGAIVR GFDTRSAARE QVQSLGAEFI
EVEIEEDGSG GGGYAKTMSK EFIEAEMKLF MEQCKEVDIV ITTALIPGKP APTLITEEMV
NAMKPGSVIV DLAAEAGGNV ESTVPNEVVS VGGVTVIGYT DFPSRLPTQA STLYSNNITK
YLLSMSPKEG HFGIDLKDEV VRRSIVTHNG EVVPPLPPLA PPAPAAKPAE IVKEEVVALT
PWQKATREVA TITGGMTTAL ALGKMTGPIF MGNLFTFSLA GLIGYRVVWG VAPALHSPLM
SVTNAISGMV GIGGFFIMGG GYLPQTIPQV LGAASVLLAF VNVSGGFVIT KRMLDMFRRP
TDPPEYPWLY AVPGVLFGGG FLAASATGMA GIVQAGYLAS SLLCIGSLTG LASQATARTG
NLLGILGVSS GVLASLAAVG FSPETLIQCL TVAGVGSAIG ALLGRRITPT ELPQMVAALH
SVVGLAAVLT SIGSVMAGLA HADMLHLVTG YLGVLIGGVT FTGSIIAFLK LSGKMSSRPV
RLPGGSPLVN STLMTANMAT FAGFLAFAPG APAIAATCLG VNTALSFAKG YTTTAAIGGA
DMPVVITVLN AYSGFALVAE GFMLNSPILT TVGSLIGVSG SILSYIMCVA MNRSLTNVLF
GGIAAPAPTS SNEVVGEMTK TSIEETVDML RNAQNVVIVV GYGMAVAKAQ YPIAEIVSTL
RAQGVNVKFA IHPVAGRMPG QCNVLLAEAS VPYDVVLEMD EINEEGFDDV DLTLVIGAND
TVNPIALQPD SPIAGMPIID AYKSKQVIVM KRGMGSGYAD LVNPMFYAEN TKMLFGDAKT
SCDAIKAALD AAPK
//
