ID A0A011QHD8_9PROT Unreviewed; 158 AA.
AC A0A011QHD8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ECO:0000313|EMBL:EXI88727.1};
GN ORFNames=AW12_01860 {ECO:0000313|EMBL:EXI88727.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI88727.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI88727.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient.
CC {ECO:0000256|ARBA:ARBA00025189}.
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:EXI88727.1}.
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DR EMBL; JEMZ01000096; EXI88727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011QHD8; -.
DR STRING; 1454005.AW12_01860; -.
DR PATRIC; fig|1454005.3.peg.1797; -.
DR Proteomes; UP000020878; Unassembled WGS sequence.
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:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 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, ECO:0000256|RuleBase:RU004464};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356,
KW ECO:0000256|RuleBase:RU004464}; Membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356,
KW ECO:0000256|RuleBase:RU004464};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW Oxidoreductase {ECO:0000313|EMBL:EXI88727.1};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW Reference proteome {ECO:0000313|Proteomes:UP000020878};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01356};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_01356}.
FT DOMAIN 37..146
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ SEQUENCE 158 AA; 17494 MW; D00F0CB656475608 CRC64;
MGIEGILQEG FVTTTADKLI NYVRTGSLWP MTFGLACCAI EMIHAGCSRY DLDRFGIVFR
PSPRQSDVMV VAGTLTNKMA PAMRKVYDQM AEPRWVVSMG SCANGGGYYH YSYSVVRGCD
RIVPVDIYVP GCPPTAEALI YGLIQLQNKI RRTNTIAR
//