ID A0A0D8D3X1_9GAMM Unreviewed; 212 AA.
AC A0A0D8D3X1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SG35_02460 {ECO:0000313|EMBL:KJE43506.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE43506.1};
RN [1] {ECO:0000313|EMBL:KJE43506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE43506.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|HAMAP-Rule:MF_01356,
CC ECO:0000256|RuleBase:RU004464}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJE43506.1}.
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DR EMBL; JYNI01000003; KJE43506.1; -; Genomic_DNA.
DR RefSeq; WP_044830777.1; NZ_CP059735.1.
DR AlphaFoldDB; A0A0D8D3X1; -.
DR STRING; 485447.SG35_02460; -.
DR PATRIC; fig|485447.4.peg.2825; -.
DR OrthoDB; 9786737at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12280; -; 1.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR NCBIfam; TIGR01957; nuoB_fam; 1.
DR PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR11995:SF36; NADH-QUINONE OXIDOREDUCTASE SUBUNIT B; 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|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01356};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01356};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01356};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01356}; Membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01356};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01356};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01356};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_01356}.
FT DOMAIN 55..162
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ SEQUENCE 212 AA; 24098 MW; 5E3D8498EF3D3C60 CRC64;
MEWSLTKAKL DEFMGQSKAL QEEELNRNVF MARLDDMINW GRKNSIWPFN FGLSCCYVEM
ATSFTSRHDI ARFGAEVIRA TPRQADLMVI SGTCFRKMAP VIQHLYEQLL EPRWIISMGS
CANSGGMYDI YSVVQGVDKF IPVDVYVPGC PPRPEALLEG LLLLQNNIQH QPRPLSWVVG
EQGVSQIAKP SLRDIKHEHR IQVTNLDSPD NC
//
