ID R4YXD2_9ACTN Unreviewed; 185 AA.
AC R4YXD2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01351};
DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
DE AltName: Full=NDH-1 subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
GN Name=nuoI {ECO:0000256|HAMAP-Rule:MF_01351,
GN ECO:0000313|EMBL:CCM63064.1};
GN ORFNames=BN381_160029 {ECO:0000313|EMBL:CCM63064.1};
OS Candidatus Microthrix parvicella RN1.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Microthrixaceae; Microthrix.
OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM63064.1, ECO:0000313|Proteomes:UP000018291};
RN [1] {ECO:0000313|EMBL:CCM63064.1, ECO:0000313|Proteomes:UP000018291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN1 {ECO:0000313|EMBL:CCM63064.1,
RC ECO:0000313|Proteomes:UP000018291};
RX PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT based on genomic and metagenomic analyses.";
RL ISME J. 7:1161-1172(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_01351}.
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_01351};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01351};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01351};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01351}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01351}.
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:CCM63064.1}.
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DR EMBL; CANL01000008; CCM63064.1; -; Genomic_DNA.
DR RefSeq; WP_012225125.1; NZ_HG422565.1.
DR AlphaFoldDB; R4YXD2; -.
DR STRING; 1229780.BN381_160029; -.
DR GeneID; 78313419; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_4_2_11; -.
DR OrthoDB; 9808559at2; -.
DR Proteomes; UP000018291; 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:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.3270; -; 1.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10849:SF37; NADH-QUINONE OXIDOREDUCTASE SUBUNIT I 2; 1.
DR Pfam; PF00037; Fer4; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01351};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01351};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01351}; Membrane {ECO:0000256|HAMAP-Rule:MF_01351};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01351}; NAD {ECO:0000256|HAMAP-Rule:MF_01351};
KW Oxidoreductase {ECO:0000313|EMBL:CCM63064.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
KW Reference proteome {ECO:0000313|Proteomes:UP000018291};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}.
FT DOMAIN 58..87
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 107..136
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 26..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
SQ SEQUENCE 185 AA; 20935 MW; 9E37355F04F07FFA CRC64;
MPPKPPLQGL VKGLKLTLRT AMETMFPDGP LKPPSPAKGA ATVQYPREKE SPAPRARGVI
ALHEENCTAC MLCARECPDW CIYIEGHKTL APPRRPGGKP RSVNDLDRFD IDYSLCMYCG
ICVEVCPFEA LFWTPEYEYS EVRIADLLHD KERLGEWFET VPDFESYEAG AQMKQKKVPR
KESSE
//
