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Database: UniProt
Entry: A0A2V5KZU9_9MICC
LinkDB: A0A2V5KZU9_9MICC
Original site: A0A2V5KZU9_9MICC 
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
//
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