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Database: UniProt
Entry: A0A151MX72_ALLMI
LinkDB: A0A151MX72_ALLMI
Original site: A0A151MX72_ALLMI 
ID   A0A151MX72_ALLMI        Unreviewed;      1111 AA.
AC   A0A151MX72;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 16.
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:KYO29065.1};
GN   ORFNames=Y1Q_0009871 {ECO:0000313|EMBL:KYO29065.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO29065.1};
RN   [1] {ECO:0000313|EMBL:KYO29065.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO29065.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(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   -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005624}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO29065.1}.
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DR   EMBL; AKHW03004724; KYO29065.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151MX72; -.
DR   Proteomes; UP000050525; 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; 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:UP000050525};
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        497..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        526..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        618..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        643..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        667..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        693..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        724..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        761..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        800..818
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        879..900
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..220
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          229..393
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   1111 AA;  117215 MW;  86E3E073FDF2CCAC CRC64;
     MRQDCGWDSM CGSPCQKIPG NMASLLRVVV SSCSNPLFSN VMSCKIRTVK IPCLRTLQTH
     QVLWCQAPIK PGIPYKQLTV GVPKEIFQNE KRVSLSPAGV QALVKQGFNV VVESGAGEAS
     KFSDDHYREV GAKIQGTKEV LASDLIVKVR APVVNPDLGI HEADLFKTAA TLISFIYPAQ
     NPDLLKKLAE RKTTVLAMDQ VPRVTIAQGY DALSSMANIA GYKAVVLAAN NFGRFFTGQI
     TAAGKVPPAK VLIIGGGVAG LAAAGAAKSM GAVVRGFDTR AAALEQFKSL GAEPLEVDLK
     ESGEGQGGYA KEMSKEFIEA EMQLFAKQCQ DVDIIISTAL IPGKKAPILF RKDMVELMKE
     GSVVVDLAAE AGGNFETTKP GDLYIHKGVT HIGYTDLPSR MATQASTLYS NNIIKLLKAI
     SPDKENFHYD VKDEFDYGTL DHVIRGTVVM KDGRLIFPAP PPKNIPQAAP VKQKTVAELE
     AEKASTVTPF RKTMTSATAY TAGLASLLGL GIAAPNSAFT QMVTTFGLAG IVGYHTVWGV
     TPALHSPLMS VTNAISGLTA VGGLVLMGGS YLPENIPQGL AVLSAFVSSV NIAGGFLVTQ
     RMLDMFKRPT DPPEYNYLYF LPAGVFVGGY SAALYGGYNI EQMMYLGSGL CCVGALAGLS
     TQGTARLGNT LGMIGVAGGL AATLGGLTPS PELLAQMSGA MTLGGTIGLT IAKRIQISDL
     PQLVAAFHSL VGLAAVLTCV AEYMIEYPHF ETDPAANLTK IVAYLGTYIG GVTFSGSLVA
     YGKLQGILNS APLLLPGRHL LNASLLAASV GGMVPYMIDP SYTTGLACLG SVSTLSAIMG
     VTLTAAIGGA DMPVVITVLN SYSGWALCAE GFLLNNNLLT IVGALIGSSG AILSYIMCVA
     MNRSLANVIL GGYGTTSTAG GKPMEITGTH TEINLENAVE MIKEANNIII TPGYGLCAAK
     AQYPIADLVK MLTEQGKHVR FGIHPVAGRM PGQLNVLLAE AGVPYDIVLE MDEINEDFPE
     TDLVLVIGAN DTVNSAAQED PNSIIAGMPV LEVWKSKQVI VMKRSLGVGY AAVDNPIFYK
     PNTAMLLGDA KKTCDALQAK VRESYQKNRE H
//
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