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
//