ID A0A0C9MUR6_SPHPI Unreviewed; 375 AA.
AC A0A0C9MUR6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntAA {ECO:0000313|EMBL:GAN14426.1};
GN ORFNames=SP6_39_00010 {ECO:0000313|EMBL:GAN14426.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN14426.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN14426.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN14426.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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 -!- 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:GAN14426.1}.
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DR EMBL; BBJS01000039; GAN14426.1; -; Genomic_DNA.
DR RefSeq; WP_007407166.1; NZ_BBJS01000039.1.
DR AlphaFoldDB; A0A0C9MUR6; -.
DR GeneID; 78527848; -.
DR Proteomes; UP000032025; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 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.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 6..140
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..315
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 375 AA; 38690 MW; 470739C3C0D2F7B4 CRC64;
MPSRIAVLLE SAQAERRVAA TPETVRKLIA LGATVAIESG AGREAGIADG EYEQAGATVA
DRATVLAGAD IVLAVQAPDP ATLAGSVPGA WVVAAFDPFR QRERVTGYAA AGLEALAMDW
MPRITRAQSM DILSSQSNLA GYKAVLEAAS AYGRAFPMMM TAAGTIPAAR VFVMGVGVAG
LQAIATARRL GAQVSATDVR SATREQIQSL GAKPIFVEGV AGIEGEGAGG YAGETSEEYR
AAQAELVAGH IAKQDIVITT ALIPGRPAPR LVSDAQIATM RPGSVIVDLA VEAGGNVEGA
VLGEVVQRHG VTIVGHRNMP SLLAADASAL FARNLYNFLA AFWDKEAARP VLDAEIGDAI
RLTKGSQVVN PRLSA
//