ID Q8YD54_BRUME Unreviewed; 429 AA.
AC Q8YD54;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN OrderedLocusNames=BMEII0323 {ECO:0000313|EMBL:AAL53565.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL53565.1, ECO:0000313|Proteomes:UP000000419};
RN [1] {ECO:0000313|EMBL:AAL53565.1, ECO:0000313|Proteomes:UP000000419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094
RC {ECO:0000313|Proteomes:UP000000419};
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA Haselkorn R., Kyrpides N., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53565.1; -; Genomic_DNA.
DR PIR; AB3550; AB3550.
DR RefSeq; WP_004682363.1; NZ_CP007762.1.
DR AlphaFoldDB; Q8YD54; -.
DR SMR; Q8YD54; -.
DR GeneID; 29595944; -.
DR KEGG; bme:BMEII0323; -.
DR KEGG; bmel:DK63_2918; -.
DR PATRIC; fig|224914.52.peg.3060; -.
DR eggNOG; COG3288; Bacteria.
DR Proteomes; UP000000419; Chromosome II.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:AAL53565.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 6..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..314
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 380..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 44599 MW; 0530649A75C71473 CRC64;
MAQTLYIPKE SDPNETRVAG SAETVKKFIA LGFDVVVEKG AGEKSRIPDA EFAAAGARIG
TAVDAKTADV ILKVRRPGDA ELKAYKSGAA LFAMLDPYGH EDAVAALARA GISAFTMEFI
PRITRAQVMD VLSSQANLAG YQAVIDAAEV YDRAMPMMMT AAGTVPAAKV FVMGAGVAGL
QAIATARRLG AVVTATDVRP AAKEQVASLG AKFIAVEDDE FKAAETAGGY AKEMSKDYQA
KQAALVADHI AKQDIVITTA LIPGRPAPRL VSKEMVASMR PGSVLVDLAV ERGGNVEGAV
PGEIADVNGV KIVGYLNVPG RIAASASQLY ARNLIAFVET LVDKESKVLK IDPEEELVKA
TLLTHQGRIL HPAFAKAETA PAAVTEKAEK PKAAPKAPPK AAAKPAKKAP AKAAKKPSSP
KSPVDGGEA
//
