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Database: UniProt
Entry: A0A2H3KJL0_9CHLR
LinkDB: A0A2H3KJL0_9CHLR
Original site: A0A2H3KJL0_9CHLR 
ID   A0A2H3KJL0_9CHLR        Unreviewed;       180 AA.
AC   A0A2H3KJL0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=A9Q02_03260 {ECO:0000313|EMBL:PDV98113.1};
OS   Candidatus Chloroploca asiatica.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Candidatus Chloroploca.
OX   NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV98113.1, ECO:0000313|Proteomes:UP000220922};
RN   [1] {ECO:0000313|EMBL:PDV98113.1, ECO:0000313|Proteomes:UP000220922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7-9 {ECO:0000313|EMBL:PDV98113.1,
RC   ECO:0000313|Proteomes:UP000220922};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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:PDV98113.1}.
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DR   EMBL; LYXE01000110; PDV98113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3KJL0; -.
DR   OrthoDB; 9786737at2; -.
DR   Proteomes; UP000220922; 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.
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   Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220922};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01356}.
FT   DOMAIN          38..147
FT                   /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF01058"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         104
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         133
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   180 AA;  19938 MW;  E4BEAC4285FAD86B CRC64;
     MGLETKAGDL GVVTTSLEYV VNWGRTNAMW PLLFGLACCA IEMMGAQSPN YDMSRFGMEI
     NRASPRQADL MIVAGRVSRK MAPVVRRLYD QMSEPKWVVA MGDCASCGGI FNNYAIVQGV
     DEIVPVDVYV AGCPPRPEAL IDGIMMLHEK VKREKISGIK EQPLRLEQPL IQQVDVKKYG
//
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