ID D6ZIJ7_MOBCV Unreviewed; 400 AA.
AC D6ZIJ7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN OrderedLocusNames=HMPREF0573_10227 {ECO:0000313|EMBL:ADI66546.1};
OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS vaginalis).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI66546.1, ECO:0000313|Proteomes:UP000006742};
RN [1] {ECO:0000313|Proteomes:UP000006742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43063 / DSM 2711 / V125
RC {ECO:0000313|Proteomes:UP000006742};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) 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};
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DR EMBL; CP001992; ADI66546.1; -; Genomic_DNA.
DR AlphaFoldDB; D6ZIJ7; -.
DR STRING; 548479.HMPREF0573_10227; -.
DR KEGG; mcu:HMPREF0573_10227; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_11; -.
DR Proteomes; UP000006742; Chromosome.
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:UP000006742};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 18..161
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 170..335
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 400 AA; 42583 MW; 63FCD7AACB04D07C CRC64;
MSCVYNEVFA EGFKMIIGVP KEIMNGEDRV AATPETVADM VGKGLTVLVE TGAGEGSFFH
DPEYVSAGAE MVSDPEEIYQ RADLILKVKE PLFNEAKGRS EVSMMHKGQY LITFIHPAAP
PNHEMVKEMA AQGVISLTLD GVPRISRAQN LDALTSMSTC AGYKGILLAA NYQPSFMPLI
HSAIGRIDPL KVLVVGVGVG GLQALATAKR LGAVVYAADI RPMASEQATS LGAKPVELGV
DPEKAIGEGG YAQALPEDEL VKERAALAQV IPDMDIIFAS ALVPGHLAPR LITEDMVKTM
KPGSVIVDIS IDQGGNCEIT PPGKVEVKHH VTLVGIKNIP GMLPKSSTFM FAKNIANFVD
FLVKDGQIVL DRSDEIIAKT LTTIDGEIVH VGAREAMGLA
//
