ID A0A094KW61_ANTCR Unreviewed; 1086 AA.
AC A0A094KW61;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=N321_04085 {ECO:0000313|EMBL:KFZ61527.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ61527.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ61527.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ61527.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KL354984; KFZ61527.1; -; Genomic_DNA.
DR RefSeq; XP_010169577.1; XM_010171275.1.
DR AlphaFoldDB; A0A094KW61; -.
DR GeneID; 104527535; -.
DR KEGG; acar:104527535; -.
DR CTD; 23530; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000053620; 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:UP000053620};
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 501..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..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 646..666
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; 113951 MW; 61F150A83DDEBE3C CRC64;
MASLLRIAVS GCSTPVFGTV LPPKLHSAKM PCLRMFRTHQ MLRSEAAPKP GIPYKQLTVG
VPKEIFENEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK FSDDHYREVG AKIQGTKEVL
ASDLVVKVRA PMFNSSLGVH EADLFKTAAT LISFIYPAQN PELLKKLGEK KTTVLAMDQV
PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKV LIIGGGVAGL
ASAGAAKSMG AVVRGFDTRA AALEQFKSLG AEPLEVDIKE SGEGQGGYAK EMSKEFIEAE
MKLFAKQCQD VDIIITTALI PGKKAPVLFK KNMIESMKEG SVVVDLAAEA GGNIETTKPG
ELYVHKGVTH IGYTDLPSRM ATQASTLYSN NIIKLLKAIS PDKENFYFDP KDEFDYGTLD
HVIRGTVVMK DGKVIFPAPP PNNIPQGAPV KQKTVAELEA EKAATITPFR KTMTSASVYT
AGLSGMLGLG LVAPNTAFTQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV
GGLVLMGGKY LPENAPQILA VLSAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
PGGVFVGGYT AALSGGYNIE QMMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA
ATLGGLKPSP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCVA
EYMIEYPHFA TDPAANLTKI VAYLGTYIGG VTFSGSLVAY GKLQGILNSA PLLLPGRHAL
NAGLLAASVG GMIPYMIVPS 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
//
