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Database: UniProt
Entry: D8JG94_ACISD
LinkDB: D8JG94_ACISD
Original site: D8JG94_ACISD 
ID   D8JG94_ACISD            Unreviewed;       375 AA.
AC   D8JG94;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   OrderedLocusNames=AOLE_16625 {ECO:0000313|EMBL:ADI92212.1};
OS   Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI92212.1, ECO:0000313|Proteomes:UP000000392};
RN   [1] {ECO:0000313|EMBL:ADI92212.1, ECO:0000313|Proteomes:UP000000392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16667 / KCTC 23045 / DR1
RC   {ECO:0000313|Proteomes:UP000000392};
RX   PubMed=20639327; DOI=10.1128/JB.00722-10;
RA   Jung J., Baek J.H., Park W.;
RT   "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT   DR1.";
RL   J. Bacteriol. 192:4794-4795(2010).
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}.
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DR   EMBL; CP002080; ADI92212.1; -; Genomic_DNA.
DR   RefSeq; WP_004794594.1; NZ_VEIV01000005.1.
DR   AlphaFoldDB; D8JG94; -.
DR   GeneID; 9383763; -.
DR   KEGG; acd:AOLE_16625; -.
DR   eggNOG; COG3288; Bacteria.
DR   HOGENOM; CLU_003376_2_1_6; -.
DR   OMA; YFPMLMT; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000000392; Chromosome.
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; IPR008142; AlaDH/PNT_CS1.
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; PS00836; ALADH_PNT_1; 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          4..136
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          145..316
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   375 AA;  39917 MW;  1BC87428DBDB17CE CRC64;
     MQIGIPTETV VGENRVAATP ETVKKLISAG HSVVIERGAG VKAAYIDSAY EQVGATITDD
     AYTGSQIILK VRAPQGGEIQ KLAANTAVVA MFDPYRNTEL DQFANQQVSA FALELLPRTL
     SRAQNMDVLS SQANLSGYKS VLLAAAEYQR MFPMLMTAAG TVKPARVVIM GVGVAGLQAI
     ATAKRLGAIV EATDLRPTAK DQVESLGGKW LDVPMSEEEQ QRAADAAKNG YGWMPGEQYI
     KDQAAIVDKA VSNADIVITT ALLPGRDAPR LIKAETVAKM KPGSVILDMA VETGGNVEGS
     KVGETVFTEN GVKILGIPNI PATVATEASA LYARNVFNFV ETLFDKEKNF AINQEDEIQK
     ALLVTHGGQV LLKRG
//
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