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Database: UniProt
Entry: A0A0M2Q389_PROHO
LinkDB: A0A0M2Q389_PROHO
Original site: A0A0M2Q389_PROHO 
ID   A0A0M2Q389_PROHO        Unreviewed;       537 AA.
AC   A0A0M2Q389;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   ORFNames=PROH_03495 {ECO:0000313|EMBL:KKJ01414.1};
OS   Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC   Prochlorotrichaceae; Prochlorothrix.
OX   NCBI_TaxID=317619 {ECO:0000313|EMBL:KKJ01414.1, ECO:0000313|Proteomes:UP000034681};
RN   [1] {ECO:0000313|EMBL:KKJ01414.1, ECO:0000313|Proteomes:UP000034681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CALU 1027 {ECO:0000313|EMBL:KKJ01414.1};
RA   Shanker A., Yadav P., Khan S., Sharma V.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKJ01414.1, ECO:0000313|Proteomes:UP000034681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CALU 1027 {ECO:0000313|EMBL:KKJ01414.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC       respiration and ATP hydrolysis and functions as a proton pump across
CC       the membrane. {ECO:0000256|ARBA:ARBA00003943}.
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: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689}.
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:KKJ01414.1}.
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DR   EMBL; AJTX02000002; KKJ01414.1; -; Genomic_DNA.
DR   RefSeq; WP_017714129.1; NZ_KB235941.1.
DR   AlphaFoldDB; A0A0M2Q389; -.
DR   STRING; 317619.GCA_000332315_03978; -.
DR   eggNOG; COG3288; Bacteria.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000034681; 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   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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR026255; NADP_transhyd_a.
DR   InterPro; IPR024605; NADP_transhyd_a_C.
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; PF12769; PNTB_4TM; 1.
DR   PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 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   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:UP000034681};
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        429..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        479..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        506..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..168
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          177..341
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  56228 MW;  1B4C942E41E3FCBB CRC64;
     MTIALEQPNT APAATPGDGV ISPKIIGVPQ EIFPGECRVA ATPDTAKRLQ KMGFEVWVES
     GAGAAASFDD AAYAQAGCKI IEDTAQLWQG SDVVLKVRPP APNPAQGCHE ADLLREGGTL
     ISFIWPAQNP ELLEHLGQRK ATVLAMDVVP RISRAQKMDA LSSMANIAGY RAVIEAANQF
     GRFFTGQITA AGKVPPCKVL VIGAGVAGLA AIGAAKSLGA VVRAFDTRPV VKEQVESMGA
     EFLELEFEED GTGSGGYAKT MSKEFIEAEM ALFADQARDV DIIITTALIP GKTAPVLITT
     AMVESMKAGS VVVDLAAEQG GNCQVTRPNE IYDYQGVKII GLTDLPSRMA SQSSQLYGTN
     LCHLLSDMGG SQDYRVDLED EVVRGALVLH DGALTWPAPK PATPPPAPAK AVNPTIAATP
     TADSGNGNLL WFGVAALALV GIGIGAPPSF LSHFTVFVLA CFVGWQVVWN VTPALHTPLM
     SVTNAISGII IIGGMLQISG PMGSPTMILG AIAILVGTIN ISGGFLVTQR MLQMFRK
//
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