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Database: UniProt
Entry: A0A091Q7M4_HALAL
LinkDB: A0A091Q7M4_HALAL
Original site: A0A091Q7M4_HALAL 
ID   A0A091Q7M4_HALAL        Unreviewed;      1086 AA.
AC   A0A091Q7M4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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|EMBL:NWZ53302.1};
GN   ORFNames=HALALB_R13619 {ECO:0000313|EMBL:NWZ53302.1}, N329_06638
GN   {ECO:0000313|EMBL:KFQ05604.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ05604.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ05604.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ05604.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NWZ53302.1, ECO:0000313|Proteomes:UP000585422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0040 {ECO:0000313|EMBL:NWZ53302.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NWZ53302.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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   -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005624}.
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DR   EMBL; KK657007; KFQ05604.1; -; Genomic_DNA.
DR   EMBL; VZSQ01000096; NWZ53302.1; -; Genomic_DNA.
DR   RefSeq; XP_009919164.1; XM_009920862.1.
DR   GeneID; 104319218; -.
DR   KEGG; hald:104319218; -.
DR   CTD; 23530; -.
DR   OrthoDB; 313696at2759; -.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
DR   Proteomes; UP000585422; 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; 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: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; PS00836; ALADH_PNT_1; 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:UP000054379};
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        476..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        505..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        530..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        557..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        597..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        622..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        672..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        703..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        740..760
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        780..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        858..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..199
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          208..372
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   1086 AA;  113944 MW;  3F4C4B14B546EBB6 CRC64;
     MASLLRIAVS GCSTPVFGNV LPPKVHSAKM PCLRMFRTHQ MLTSQAAPKP GIPYKQLTVG
     VPKEIFENEK RVALSPAGVQ ALIKQGFNVV VESGAGEASK FSDDHYREVG AKIQGTKEVL
     ASDLIVKVRA PIYNSALGVH EADLFKTAAT LVSFIYPAQN PDLLKKLAEK KTTVLAMDQV
     PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKV LIIGGGVAGL
     ASAGAAKSMG AVVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE
     MKLFAKQCQD VDIIITTALI PGKKAPILFK KDMIELMKEG SVVVDLAAEA GGNIETTKPG
     EMYVHKGVTH IGYTDLPSRM ATQASTLYSN NIIKLLKAIS PDKENFYFDP KDEFDYGTLD
     HVIRGTVVMK DGKVIFPAPP PNNVPQGPPV KQKTVAELEA EKAATITPFR KTMTSASLYT
     AGLAGMLGLG LVAPNTAFTQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV
     GGLVLMGGNY LPENTPQSLA VLSAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
     PGGVFVGGYA AALNGGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA
     ATLGGLKPSP ELLAQMSGAM ALGGTIGLTI AKRIQITDLP QLVAAFHSLV GLAAVLTCVA
     EYMIEYPHFA TDPAANLTKV VAYLGTYIGG VTFSGSLIAY GKLQGILNSA PLLLPGRHAL
     NAGLLAASVG GMVPYMIDPS YTTGITCLGS VSALSAIMGV TLTAAIGGAD MPVVITVLNS
     YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG
     KPMEITGTHT EINVDNAIEM IKEANNIIIT PGYGLCAAKA QYPIADLVKM LREQGKNVRF
     GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINEDFPET DLVLVIGAND TVNSAAQEDP
     NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV
     RESYQS
//
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