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Entry: A0A073K2C6_9BACI
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ID   A0A073K2C6_9BACI        Unreviewed;       366 AA.
AC   A0A073K2C6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000256|HAMAP-Rule:MF_01358};
GN   ORFNames=BAMA_01310 {ECO:0000313|EMBL:KEK21434.1};
OS   Bacillus manliponensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK21434.1, ECO:0000313|Proteomes:UP000027822};
RN   [1] {ECO:0000313|EMBL:KEK21434.1, ECO:0000313|Proteomes:UP000027822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK21434.1,
RC   ECO:0000313|Proteomes:UP000027822};
RA   Lai Q., Liu Y., Shao Z.;
RT   "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT   1A00708).";
RL   Submitted (JUN-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. 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_01358}.
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_01358};
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_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01358}.
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:KEK21434.1}.
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DR   EMBL; JOTN01000001; KEK21434.1; -; Genomic_DNA.
DR   RefSeq; WP_034635343.1; NZ_JOTN01000001.1.
DR   AlphaFoldDB; A0A073K2C6; -.
DR   STRING; 574376.BAMA_01310; -.
DR   eggNOG; COG0649; Bacteria.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000027822; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Oxidoreductase {ECO:0000313|EMBL:KEK21434.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027822};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01358}.
FT   DOMAIN          120..365
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   366 AA;  41727 MW;  3619373C81C2F06F CRC64;
     MIRTEEMLLN VGPQHPSTHG VFRLVIKIDG ETIKEATPVI GYLHRGTEKI AENLQYTQII
     PYTDRMDYLS AMTNNYVVCH AVETMMELEI PERAEYLRVL AMELGRVASH LVWWGTNLLD
     IGAVSPFLYA FREREMIINL LNELCGARLT FNYMRVGGVK WDAPDGWIEK VREFVPYMRE
     QLAGYHDLVS GNEIFLNRVK DVGIYSAEEA LSYSLSGANL RCTGVNWDLR KDEPYSIYNR
     FHFDVPVGEK GDALDRYVCR MQEIEESLKI IEQAVEQFPK EGAILAKVPR IIKAPKGEAF
     VRIESPRGEI GCYIASDGKK EPYRLKFRRP SFYNLQILPE LLKGENIANL ITILGGIDIV
     LGEVDG
//
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