ID A0A3Q0GVM7_ALLSI Unreviewed; 901 AA.
AC A0A3Q0GVM7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=NNT {ECO:0000313|RefSeq:XP_025063497.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025063497.1};
RN [1] {ECO:0000313|RefSeq:XP_025063497.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR RefSeq; XP_025063497.1; XM_025207712.1.
DR AlphaFoldDB; A0A3Q0GVM7; -.
DR Proteomes; UP000189705; Unplaced.
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:SF22; NAD(P) TRANSHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
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 488..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..211
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 220..384
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 901 AA; 95865 MW; 1377C04A06263607 CRC64;
MRGSPSQKIP GNMASLLRVV VSSCSNPLFS NVMSCKIRTV KIPCLRTFQT HQVLWCQAPI
KPGIPYKQLT VGVPKEIFQN EKRVSLSPAS VQALVKQGFN VVVESGAGEA SKFSDDHYRE
VGAKIQGTKE VLASDLIVKV RAPVVNPDLG IHEADLFKTA ATLISFIYPA QNPDLLKKLA
ERKTTVLAMD QVPRVTIAQG YDALSSMANI AGYKAVVLAA NHFGRFFTGQ ITAAGKVPPA
KVLIIGGGVA GLAAAGAAKS MGAVVRGFDT RAAALEQFKS LGAEPLEVDL KESGEGQGGY
AKEMSKEFIE AEMQLFAKQC QDVDIIISTA LIPGKKAPIL FRKDMVELMK EGSVVVDLAA
EAGGNFETTK PGDLYIHKGV THIGYTDLPS RMATQASTLY SNNIIKLLKA ISPDKENFHY
DVKDEFDYGT LDHVIRGTVV MKDGRLIFPA PPPKNIPQAA PVKQKTVAEL KAEKASTVTP
FRKTMTSATA YTAGLASLLG LGIAAPNSAF TQMVTTFGLA GIVGYHTVWG VTPALHSPLM
SVTNAISGLT AVGGLVLMGG SYLPENIPQG LAVLSAFVSS VNVAGGFLVT QRMLDMFKRP
TDPPEYNYLY FLPAGVFVGG YSAALYGGYN IEQGVTLTAA IGGADMPVVI TVLNSYSGWA
LCAEGFLLNN NLLTIVGALI GSSGAILSYI MCVAMNRSLA NVILGGYGTT STAGGKPMEI
TGTHTEINLE NAVEMIKEAN NIIITPGYGL CAAKAQYPIA DLVKMLTEQG KHVRFGIHPV
AGRMPGQLNV LLAEAGVPYD IVLEMDEINE DFTETDLVLV IGANDTVNSA AQEDPNSVIA
GMPVLEVWKS KQVIVMKRSL GVGYAAVDNP IFYKPNTAML LGDAKKTCDA LQAKVRESYQ
K
//
