ID A0A1F0GE63_9PORP Unreviewed; 385 AA.
AC A0A1F0GE63;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=HMPREF3027_09290 {ECO:0000313|EMBL:OFO58494.1};
OS Porphyromonas sp. HMSC077F02.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1739529 {ECO:0000313|EMBL:OFO58494.1, ECO:0000313|Proteomes:UP000178655};
RN [1] {ECO:0000313|Proteomes:UP000178655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC077F02 {ECO:0000313|Proteomes:UP000178655};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2016) 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 -!- 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:OFO58494.1}.
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DR EMBL; LTSX01000011; OFO58494.1; -; Genomic_DNA.
DR RefSeq; WP_018028183.1; NZ_KV820692.1.
DR AlphaFoldDB; A0A1F0GE63; -.
DR STRING; 1739529.HMPREF3027_09290; -.
DR Proteomes; UP000178655; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 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.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000178655};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..147
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 156..321
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 385 AA; 41658 MW; 1588DA87D4530BD9 CRC64;
MIICIPKEIM HGESRVSATP ETVEKFVADG ATVYVEAGAG EPSFHHDNDY VTAGAQLLTD
TEELYQKADV ILKVKEPLFN ERLGKHEVDM MHEGQVLITF IHPASPVNHD MVRKLAKQGV
IALTLDGIPR ISRAQNLDAL TSMSTCAGYK GILLAANELA YFMPQMFTAV GQIKPAKAMV
IGVGVAGLQA LATARRLGAI TYAADIRPMA LEQATSLGAK PIETGVPAEL AIAEGGYANS
LPADVLAKER EMLFPTIKEM DIVFCSALVP GKIAPTLITE EMVKQMKPGS VIVDISIDQG
GNCEITPPGE TERKHNVTLI GIKNIPGLLP NSSTWMFAQN VYNLVKYLTK DGKIALDMSD
EICQKILVTR DHEIVHQGTL EAMNK
//
