ENDB1_SOLTU
ID ENDB1_SOLTU Reviewed; 577 AA.
AC M1BYJ7;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=External alternative NADH dehydrogenase NDB1;
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDB1;
DE Flags: Precursor;
GN Name=NDB1; ORFNames=PGSC0003DMG400021670;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
CC -!- FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes
CC the oxidation of mitochondrial NADH does not translocate protons across
CC the inner mitochondrial membrane. Calcium-dependent NAD(P)H
CC dehydrogenase. Binds calcium ions (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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; Peripheral membrane
CC protein; Intermembrane side. Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; AEWC01039998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M1BYJ7; -.
DR SMR; M1BYJ7; -.
DR STRING; 4113.PGSC0003DMT400055796; -.
DR EnsemblPlants; PGSC0003DMT400055796; PGSC0003DMT400055796; PGSC0003DMG400021670.
DR Gramene; PGSC0003DMT400055796; PGSC0003DMT400055796; PGSC0003DMG400021670.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; M1BYJ7; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1BYJ7; baseline.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS: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; ISS: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 SMART; SM00054; EFh; 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 3: Inferred from homology;
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_0000422943"
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; 65189 MW; 91652D1617F5A15A CRC64;
MRGFTYLSKV LHSHSSYSKL LVLCSVSTGG LLVYAESNVE SGKQVVEQNQ PESKKKRVVV
LGTGWGGTSF LKDVDISSYD VQVVSPRNYF AFTPLLPSVT CGTVEARSIV EPVRNIIKKR
SGEIQFWEAE CLKIDPENRT VSCRSGINDN LAGQNDFSLQ YDYLVVAVGA QVNTFNTPGV
MEHCHFLKEV EDAQRIRRTV IDCFEKSVIP GLSEEERRTN LHFVIVGGGP TGVEFAAELH
DYVYEDLVKI YPSVKDFVKI TVIQSGDHIL NTFDERISSF AEQKFQRDGI EVSTGCRVTS
VSDHFINMKV KSTGKHVEVP YGMVVWSTGV GTRPFVKDFM EQVGQEKRRI LATDEWLRVK
GCSNVYALGD CASIDQRKVM EDISAIFKAA DKDDSGTLSI EEFRDVLEDI IIRYPQVDLY
LKNKHLLEAK DLFRDSEGNE REEVDIEGFK LALSHVDSQM KSLPATAQVA AQQGTYLSRC
LNRWDQCKSN PEGPRHFKSS GRHEFLPFEY RHLGQFAPLG GDQAAAELPG DWVSMGHSTQ
WLWYSVYASK QVSWRTRYLV VGDWVRRYIF GRDSSRI
