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Database: UniProt
Entry: A0A1Y3BXB0_HELAN
LinkDB: A0A1Y3BXB0_HELAN
Original site: A0A1Y3BXB0_HELAN 
ID   A0A1Y3BXB0_HELAN        Unreviewed;       335 AA.
AC   A0A1Y3BXB0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000256|HAMAP-Rule:MF_01356};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH dehydrogenase I subunit B {ECO:0000256|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B {ECO:0000256|HAMAP-Rule:MF_01356};
GN   Name=nuoB {ECO:0000256|HAMAP-Rule:MF_01356};
GN   ORFNames=HannXRQ_Chr02g0044941 {ECO:0000313|EMBL:OTG34360.1},
GN   HannXRQ_Chr07g0201001 {ECO:0000313|EMBL:OTG21153.1},
GN   HannXRQ_Chr10g0283501 {ECO:0000313|EMBL:OTG10067.1},
GN   HannXRQ_Chr11g0326771 {ECO:0000313|EMBL:OTG07123.1},
GN   HannXRQ_CPg0579981 {ECO:0000313|EMBL:OTF84757.1};
OS   Helianthus annuus (Common sunflower).
OG   Plastid {ECO:0000313|EMBL:OTF84757.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTF84757.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTF84757.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTF84757.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone.
CC       {ECO:0000256|ARBA:ARBA00003257}.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01356}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01356};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000766};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01356};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000256|HAMAP-Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01356};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01356}. Mitochondrion
CC       membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004225}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|HAMAP-Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000256|ARBA:ARBA00008472}.
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DR   EMBL; CM007907; OTF84757.1; -; Genomic_DNA.
DR   EMBL; CM007900; OTG07123.1; -; Genomic_DNA.
DR   EMBL; CM007899; OTG10067.1; -; Genomic_DNA.
DR   EMBL; CM007896; OTG21153.1; -; Genomic_DNA.
DR   EMBL; CM007891; OTG34360.1; -; Genomic_DNA.
DR   STRING; 4232.A0A1Y3BXB0; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr02g0061501; CDS:HanXRQr2_Chr02g0061501.1; HanXRQr2_Chr02g0061501.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr02g0061511; CDS:HanXRQr2_Chr02g0061511.1; HanXRQr2_Chr02g0061511.
DR   Gramene; mRNA:HanXRQr2_Chr02g0061501; CDS:HanXRQr2_Chr02g0061501.1; HanXRQr2_Chr02g0061501.
DR   Gramene; mRNA:HanXRQr2_Chr02g0061511; CDS:HanXRQr2_Chr02g0061511.1; HanXRQr2_Chr02g0061511.
DR   Proteomes; UP000215914; Chloroplast.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.12280; -; 1.
DR   Gene3D; 1.20.58.1610; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 1.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   NCBIfam; TIGR01957; nuoB_fam; 1.
DR   PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01356};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Plastid {ECO:0000313|EMBL:OTF84757.1};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01356};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000313|EMBL:OTF84757.1}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          153..263
FT                   /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF01058"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         218
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         249
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   335 AA;  38017 MW;  4AEC3B6551528B14 CRC64;
     MFLLYEYDIF WAFLIISSLI PILVFFISGF LAPSSKGPEK LSSYESGIEP IGDAWLQFRI
     RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFVEALIF VLILIVGLIV MNSIEFPLFH
     RTTQNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR YGLVPRSSPR
     QADLILTAGT VTMKMAPSLV RLYEQMPEPK YVIAMGACTI TGGMFSTDSY STVRGVDKLI
     PVDVYLPGCP PKPEAIIDAI TKLRKKISRE IYPDRIMSQR ENRCFTTNHK FQVGHSIHTG
     NYDQGFLYQP PSTSEIPPET FFKYKSSVSS HELVN
//
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