ID A0A094ZLN2_SCHHA Unreviewed; 1090 AA.
AC A0A094ZLN2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=MS3_00009636 {ECO:0000313|EMBL:KAH9579514.1}, MS3_0015060
GN {ECO:0000313|EMBL:KAF1330615.1}, MS3_03842
GN {ECO:0000313|EMBL:KGB35585.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB35585.1};
RN [1] {ECO:0000313|EMBL:KGB35585.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
RN [2] {ECO:0000313|EMBL:KAF1330615.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=31494670;
RA Stroehlein A.J., Korhonen P.K., Chong T.M., Lim Y.L., Chan K.G.,
RA Webster B., Rollinson D., Brindley P.J., Gasser R.B., Young N.D.;
RT "High-quality Schistosoma haematobium genome achieved by single-molecule
RT and long-range sequencing.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EMBL:KAH9579514.1}
RP NUCLEOTIDE SEQUENCE.
RA Stroehlein A.J.;
RT "Chromosome-level genome assembly for S. haematobium.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAH9579514.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=35167626;
RA Stroehlein A.J., Korhonen P.K., Lee V.V., Ralph S.A., Mentink-Kane M.,
RA You H., McManus D.P., Tchuente L.T., Stothard J.R., Kaur P., Dudchenko O.,
RA Aiden E.L., Yang B., Yang H., Emery A.M., Webster B.L., Brindley P.J.,
RA Rollinson D., Chang B.C.H., Gasser R.B., Young N.D.;
RT "Chromosome-level genome of Schistosoma haematobium underpins genome-wide
RT explorations of molecular variation.";
RL PLoS Pathog. 18:0-0(2022).
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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR EMBL; AMPZ02000273; KAF1330615.1; -; Genomic_DNA.
DR EMBL; AMPZ03000008; KAH9579514.1; -; Genomic_DNA.
DR EMBL; KL250698; KGB35585.1; -; Genomic_DNA.
DR RefSeq; XP_012795350.1; XM_012939896.1.
DR AlphaFoldDB; A0A094ZLN2; -.
DR STRING; 6185.A0A094ZLN2; -.
DR EnsemblMetazoa; XM_012939896.2; XP_012795350.1; MS3_0015060.
DR GeneID; 24591424; -.
DR KEGG; shx:MS3_00009636; -.
DR CTD; 24591424; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000471633; 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 3: Inferred from homology;
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:UP000471633};
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 527..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 783..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..194
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 203..367
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1090 AA; 115053 MW; 5CFBC5209D743FFE CRC64;
MAAVFLVLHS PTAIQSHRLV HLKSVSLVHR LYTTRPESCQ LGVAFNTLRI GIPKESFIDE
KRVSVTPQTA NLFSKCGFNV FVQTGAGVNS NFLDSDYIKA GAKIITDSVE SLYNQSDIIL
KIRPPTLNSL PNLSDEVSML RPNSTLISLI YPAKNQPLID ALSKKKVNLL ALDCIPRISR
AQSFDVLSSM ANISGYKGVI EAAGLFNRFF AGQITAAGRI PPAKVLVIGG GVAGLSAVST
AKSLGAIVRA FDTREAVREQ VESFSAEFLT VNIQESGEGG GGYAKEMSQK YLEAEMELFA
KQAKEVDIII TSALIPGKPA PKLITKDMVE SMRPGSVIVD LASESGGNVE TTVPGKLTYH
HNVAHIGYTD LPSRLPGQAS TLFSNNVANY LLSMTPPGSK DRFYLNLEDD VIRDSLILYN
GELMWPPPVR SQPKSSSKLI NSKQLSKAGS NVALQLEDSS SVFKNKLRSA ISTSVCLSGL
VGLGLYSPSS AFTTMLTTFG LSSIVGYHTV WGVTPALHSP LMSVTNAISG ITAVGGLLLM
GGGLYPSSVP ESLAASATLL SAINIGGGFV VTQRMLNMFK RPTDLPEYNY LLTIPAAGLL
GVYGYGILTV PPSLLTDMHQ TTYLASSLCC IGALTALSSQ KRCRVGNALG MIGVTSGLIS
TLGLIQPNLE LLTQMGACLT GGSLIGSIAA KRIQVTDLPQ MVALFHSLVG AAAVLTCIAN
YMVEMPHLIL DPNCYGALQL MKTVAYLGTY IGGITLTGSL IAFGKLQGIL KSTALLLPMR
NTLNASLVTL SGGCLVGLLS LGPESVLPGL GLLIGGAGVA GGISGLTLTA AIGGADMPVV
ITVLNSYSGW ALCAEGFMLN NSLMTVVGAL IGSSGAILSY IMCKAMNRSL PNVILGGYGT
SSYSGGKSMA ITGVHRQTNV SSVANYLNDF NEIIITPGYG LCVAKAQYPL AELTKELIKR
GKHVRFAIHP VAGRMPGQLN VLLAEAGVPY DIVHEMDEIN ADFSKTDLVL VIGANDTVNS
AAEEDPNSII AGMPVLRVWL AKKVVVVKRT LGVGYAAVDN PIFFKENTEM LLGDAKTICD
DLLNACRNPS
//
