ID M9RR42_9RHOB Unreviewed; 177 AA.
AC M9RR42;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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:AGI72896.1};
GN ORFNames=OA238_c28740 {ECO:0000313|EMBL:AGI72896.1};
OS Octadecabacter arcticus 238.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI72896.1, ECO:0000313|Proteomes:UP000004688};
RN [1] {ECO:0000313|EMBL:AGI72896.1, ECO:0000313|Proteomes:UP000004688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=238 {ECO:0000313|EMBL:AGI72896.1,
RC ECO:0000313|Proteomes:UP000004688};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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}.
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DR EMBL; CP003742; AGI72896.1; -; Genomic_DNA.
DR RefSeq; WP_015495944.1; NC_020908.1.
DR AlphaFoldDB; M9RR42; -.
DR STRING; 391616.OA238_c28740; -.
DR KEGG; oar:OA238_c28740; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_0_5; -.
DR OrthoDB; 9786737at2; -.
DR Proteomes; UP000004688; 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|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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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 Oxidoreductase {ECO:0000313|EMBL:AGI72896.1};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW Reference proteome {ECO:0000313|Proteomes:UP000004688};
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 56..165
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT BINDING 57
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 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ SEQUENCE 177 AA; 19444 MW; B828DD13E2DD8276 CRC64;
MGVAVGDNTA GVDRDVATQD LNKELTDKGF LVTSSADLIN WARTGSLHWM TFGLACCAVE
MMHTSMPRYD AERFGIAPRA SPRQSDVMIV AGTLTNKMAP ALRKVYDQMP EPRYVISMGS
CANGGGYYHY SYSVVRGCDR IVPVDIYVPG CPPTAEALLY GILQLQRKMR RTGTIVR
//
