ID E4UU15_ARTGP Unreviewed; 1056 AA.
AC E4UU15;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=MGYG_04608 {ECO:0000313|EMBL:EFR01605.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989824; EFR01605.1; -; Genomic_DNA.
DR RefSeq; XP_003174435.1; XM_003174387.1.
DR AlphaFoldDB; E4UU15; -.
DR STRING; 535722.E4UU15; -.
DR GeneID; 10029729; -.
DR VEuPathDB; FungiDB:MGYG_04608; -.
DR eggNOG; ENOG502QQ0A; Eukaryota.
DR HOGENOM; CLU_003376_1_0_1; -.
DR InParanoid; E4UU15; -.
DR OMA; EQCREVD; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000002669; 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; 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:UP000002669};
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 469..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 827..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..185
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 194..353
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 406..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 110468 MW; 11D50B18287870A9 CRC64;
MNNVPSPLRR ALVSYGQHAR FFSCSFRCSQ QQSNDSKLKT VPYSSLTVGV PLESFPSERR
VSLTPANVAL LLKKGFGRVL VERGAGAESQ FTDKAYTDAG ASLVGPHDAW ASDLVLKVRA
PSLNRGEVGL LKDGATAISF LYPALNRDLV EALAKRGVTS FAMDMIPRIS RAQVFDALSS
MANIAGYKAI LEASNHFGRF LPGQIPPGKV LVIGAGVAGL SAISAARRMG AIVRGFDTRP
AVREQVQSLG AEFIEVDIEE DGSGAGGYAK EMSKEFIEAE MKLFLQQSRE VDIIVTTALI
PGKPAPKLIT EEMIMAMKPG SVVVDLAAEA GGNCVMTEPG ELVVSSNGVT IIGYTDLPSR
LPTQSSTLYS NNITKFLLSM APVEKQYGVD LEDEVVRGSI VTHAGSILPP APRPAPPPPP
ATPKKDDAAV SADTAKLELT PFQKVSREVA TVTGGMGTAL ALGKFTGPLF MSNVFTAGLA
GLIGYRVVWG VTPALHSPLM SVTNAISGMV GIGGLFVMGG GYFPETIPQA LGALSVLLAF
VNVSGGFVIT KRMLDMFKRP TDPPEYPWLY AIPGVLFGGG YLAAVSTGMA GLIQAGYLVS
SILCISSISG LASQATARTG NYLGILGVAS GILASLVAVG FSPEVLAQFV GLAGIGGLVG
AVIGRRITPT ELPQMVAALH SVVGLAAVLT SIGSVLGDID HVSTLHLVTA YSGVVIGGIT
FTGSIVAFLK LSGKMASKPL AFKGRHLVNS TLLGTNMALM GGFITMAPGA PLVAAAALSA
STILSFIKGF TTTAAIGGAD MPVVITVLNA YSGFALVAEG FMLNNPLLTT VGSLIGISGS
ILSYIMCVAM NRSLTNVLFG GISSPTQAQS DHQIEGKITK TSIEETADTL ANAESVIIVV
GYGMAVAKAQ YAISEITRML RAKGRKSPIC HPSCRRPHAR TMQCPALPRL LFHTIGELVV
LEMDEINDDF SDTDVTLVIG ANDTVNPIAL EPNSSIAGMP VLHAWKSKEV IVMKRGMSSG
YADVPNPMFY MPGTKMLFGD AKTSCDAIQH ALEAHK
//
