ID A0A2V5KZU9_9MICC Unreviewed; 394 AA.
AC A0A2V5KZU9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=CVV68_22360 {ECO:0000313|EMBL:PYI64285.1};
OS Arthrobacter livingstonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI64285.1, ECO:0000313|Proteomes:UP000247832};
RN [1] {ECO:0000313|EMBL:PYI64285.1, ECO:0000313|Proteomes:UP000247832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LI2 {ECO:0000313|EMBL:PYI64285.1,
RC ECO:0000313|Proteomes:UP000247832};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) 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:PYI64285.1}.
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DR EMBL; QJVD01000059; PYI64285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5KZU9; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000247832; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
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 PRINTS; PR00368; FADPNR.
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 Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 7..142
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 151..316
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 394 AA; 39645 MW; B26CBA80173FF15B CRC64;
MTTLAVGVLS EHNSSEHRVA LDPSATARIV HSGMAVLVES GSGTDAGFDD HSFAAAGATV
TTRADVIAKC DLLASLGFPP DSVTNSLNSG QAVIGLLDPF NNLDAVRGLA DRGVILVALE
LLPRTLSRAQ AMDALSSQSS AAGYRAAIVA AESFGRYLPM MITASGTAVP AKVIVIGTGV
AGLQAIATTK RLGAVVTGYD VRAASRAEVE SLGARFLTSS VAAGTGEGGY ARSMTAEEQA
AQQQELAAAL TAFDIIITTA KVPGRIPPLL VSAQTLSALK SGTVCVDLGA SDKGGNVFGS
VDGSTHTTVD GVVVVGGGNL AAQLPTSASQ MYGRNMSAVI DSLASQGAIT VDPTDEIHAS
IVVSHHGGIT SPAVRAALNL PPLGSTDSMK VQVA
//