ID A0A087SMW3_AUXPR Unreviewed; 1256 AA.
AC A0A087SMW3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=F751_5899 {ECO:0000313|EMBL:KFM27067.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM27067.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM27067.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM27067.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
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};
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DR EMBL; KL662141; KFM27067.1; -; Genomic_DNA.
DR RefSeq; XP_011400023.1; XM_011401721.1.
DR AlphaFoldDB; A0A087SMW3; -.
DR STRING; 3075.A0A087SMW3; -.
DR GeneID; 23617290; -.
DR KEGG; apro:F751_5899; -.
DR eggNOG; KOG0737; Eukaryota.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
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; IPR027417; P-loop_NTPase.
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; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF02233; PNTB; 1.
DR SMART; SM00382; AAA; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
PE 4: Predicted;
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:UP000028924};
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 471..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 507..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 853..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..215
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 224..388
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT DOMAIN 961..1095
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 880..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 131896 MW; 6053194D3EE76B41 CRC64;
MLVLQRWSSA RGPVARGVYC ALRAFEGGSG PPNPRVILDG NPWTPAGALS STGISFPRLS
RSFAAAGTQG VPYDQLAVGV PKESFEGERR VALTPAGVAA LKKAGFKEVL VESGAGAAAN
FSDADYEAAG AVMGSTGDAF GRDIVLKIRP PHEASEVPLL QQGARLISFL HPAQNKGLVD
ALAQKRVSAL AMDCIPRTIS RAQTFDALSS MANIAGYRAV IEAANHFGRF FTGQITAAGR
VPPAKMLVIG GGVAGLSAIG TAKNMGAVVR VFDTRAAVAE QAKSLGAEFL TVNIEESGEG
GGGYAKEMSK EFIEAEMKLF AEQAKDVDII ITTALIPGKR APVLIKNHMV ESMKPGSVTV
DLAAEQGGNV ETTVPGKVVQ AGGVTCIGYT DLPSRLPTQS STLFSNNISK FLLSMGPFTG
HKGQFCIDHA DEAMVAGFHS LVGLAAVTTS IASYMAADPA HLDAVHAAST YFGTFIGAVT
LTGSAVAFGK LHGVLPSKPL ALPGKNALNL GLLAGNAAAG AAFLTTGDPG VALAALGATT
ALAGGLGAHM TASIGGADMP VVITLLNSYS GYALCAEGFM LGNDLLTTVG ALIGSSGAIL
SYIMCRAMNR SLANVILGGY ATAAAGPAAE VGGTHAEVDA HGAAEVLTSA RSVLIVPGYG
LAVAGAQYAI ADLVKRLRSK NIAVKFGIHP VAGRMPGQLN VLLAEAGVPY DIVEEMDEVN
PHMEDFDVAL VIGANDTINS AAIEDPNSVI AGMPVVEVWK AKQVIVLKRT MGTGYAGADN
PVFYKPNTQM LLGDAKTVCD QLNQKVTEAL GLSGEEWSPP MVWLGETLQK LGSAAVKMAQ
NTSRNNKSTI FEVSYLGLSL LGSWLILRWA LKQMDPTKKN VETAKQRKKA LSKRLGRPVN
TDGQYEDVSK RVIAQEVVNP AHINITLQDV GGLDHIIEDL QRNVITPMRR PELFRTSLLR
QKRGVLLYGP PGTGKTMLAK ALASECNACF INLKASTLLS KWYGDTNKLI AAVWSLAAKI
APTILFIDEV DSLLGHRRAV EHEATTAMKT EFMQLWDGFE SASDSNIVVL GATNKRDDLD
DAVLRRFSLQ YEVRLPQRAQ RETILGLLLA RHARELGAQY LDPTLMAEVE GRARGAANGT
AAPTGGSALR ALAERTEGYS GSDLTELCSM AAAIPFHDAA PTQSSPAPLS LRHFEAVLAA
YTPPSRAAQE TQAAKRRGGR GVADLPARED SMRVLAAMFN SMLGSQQQES EEEGSV
//
