ID I0KG21_9BACT Unreviewed; 172 AA.
AC I0KG21;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=FAES_5075 {ECO:0000313|EMBL:CCH03074.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH03074.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCH03074.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
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 a
CC menaquinone. 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}.
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DR EMBL; HE796683; CCH03074.1; -; Genomic_DNA.
DR RefSeq; WP_015334173.1; NC_020054.1.
DR AlphaFoldDB; I0KG21; -.
DR STRING; 1166018.FAES_5075; -.
DR KEGG; fae:FAES_5075; -.
DR PATRIC; fig|1166018.3.peg.2051; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_3_10; -.
DR OrthoDB; 9786737at2; -.
DR Proteomes; UP000011058; Chromosome.
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:CCH03074.1};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW Reference proteome {ECO:0000313|Proteomes:UP000011058};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01356}.
FT DOMAIN 42..151
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ SEQUENCE 172 AA; 19132 MW; 8B8EC447CE3038F6 CRC64;
MNAPAPSTQK AADPGVMFLT SEELLNWSRA SSLWPLTFGL ACCAIEMMQA MSASYDLERF
GIFPRPSPRQ ADIMIVSGTV TYKMADRIRR LYEQMAEPRY VISMGSCANC GGPYWQHGYH
VVKGVDRIIP VDVYVPGCPP RPEALIDGFI KLQEKIKHEQ LNRPAVSPPD NG
//
