NDB1_SOLTU
ID NDB1_SOLTU Reviewed; 577 AA.
AC Q9ST62;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial;
DE EC=1.6.5.9 {ECO:0000269|PubMed:10571867, ECO:0000269|PubMed:14731260};
DE AltName: Full=External alternative NADH dehydrogenase NDB1;
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDB1;
DE Flags: Precursor;
GN Name=NDB1;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RX PubMed=10571867; DOI=10.1046/j.1365-313x.1999.00576.x;
RA Rasmusson A.G., Svensson A.S., Knoop V., Grohmann L., Brennicke A.;
RT "Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases
RT in higher eukaryotes: two enzymes are present in potato mitochondria.";
RL Plant J. 20:79-87(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RX PubMed=14731260; DOI=10.1046/j.1365-313x.2003.01970.x;
RA Michalecka A.M., Agius S.C., Moller I.M., Rasmusson A.G.;
RT "Identification of a mitochondrial external NADPH dehydrogenase by
RT overexpression in transgenic Nicotiana sylvestris.";
RL Plant J. 37:415-425(2004).
CC -!- FUNCTION: Calcium-dependent NAD(P)H dehydrogenase. Binds calcium ions
CC (By similarity). Alternative NADH-ubiquinone oxidoreductase which
CC catalyzes the oxidation of mitochondrial NADH does not translocate
CC protons across the inner mitochondrial membrane. {ECO:0000250,
CC ECO:0000269|PubMed:10571867, ECO:0000269|PubMed:14731260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000269|PubMed:10571867, ECO:0000269|PubMed:14731260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:10571867, ECO:0000269|PubMed:14731260};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activity is calcium-dependent with a more
CC pronounced effect at higher pH. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10571867}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10571867}; Intermembrane side
CC {ECO:0000269|PubMed:10571867}. Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; AJ245862; CAB52797.1; -; mRNA.
DR RefSeq; NP_001274854.1; NM_001287925.1.
DR AlphaFoldDB; Q9ST62; -.
DR SMR; Q9ST62; -.
DR GeneID; 102591773; -.
DR KEGG; sot:102591773; -.
DR OrthoDB; 487337at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q9ST62; baseline.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; FAD; Flavoprotein; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; NADP; Oxidoreductase; Peroxisome;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..577
FT /note="External alternative NAD(P)H-ubiquinone
FT oxidoreductase B1, mitochondrial"
FT /id="PRO_0000422944"
FT DOMAIN 378..413
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 568..577
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 57..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 221..257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 577 AA; 65155 MW; 3E19B71588D4E3EF CRC64;
MRGFTYLSKV LHSHSSYSKL LVLCSVSTGG LLVYAESNVE SGKQVVEQNQ PESKKKRVVV
LGTGWGGTSF LKDVDISSYD VQVVSPRNYF AFTPLLPSVT CGTVEARSIV EPVRNIIKKR
SGEIQFWEAE CLKIDPVNRT VSCRSGINDN LAGHNDFSLQ YDYLVVAVGA QVNTFNTPGV
MEHCHFLKEV EDAQRIRRTV IDCFEKSVIP GLSEEERRTN LHFVIVGGGP TGVEFAAELH
DYVYEDLVKI YPSVKDFVKI TVIQSGDHIL NTFDERISSF AEQKFQRDGI EVSTGCRVTS
VSDHFINMKV KSTGKHVEVP YGMVVWSTGV GTRPFVKDFM EQVGQEKRRI LATDEWLRVK
GCSNVYALGD CASVDQHKVM EDISTIFEAA DKDDSGTLSV EEFRDVLEDI IIRYPQVDLY
LKNKHLLEAK DLFRDSEGNE REEVDIEGFK LALSHVDSQM KSLPATAQVA AQQGTYLARC
LNRWDQCKSN PEGPRRFKSS GRHEFLPFEY RHLGQFAPLG GDQAAAELPG DWVSMGHSTQ
WLWYSVYASK QVSWRTRYLV VGDWVRRYIF GRDSSRI
