ID NUOC_MYCS2 Reviewed; 238 AA.
AC A0QU34; I7FZB4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=NADH-quinone oxidoreductase subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NADH dehydrogenase I subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NDH-1 subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
GN Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01357};
GN OrderedLocusNames=MSMEG_2061, MSMEI_2016;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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:0000255|HAMAP-Rule:MF_01357}.
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:0000255|HAMAP-Rule:MF_01357};
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:0000255|HAMAP-Rule:MF_01357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01357};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01357};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01357}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR EMBL; CP000480; ABK70554.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38487.1; -; Genomic_DNA.
DR RefSeq; WP_011728124.1; NZ_SIJM01000021.1.
DR RefSeq; YP_886422.1; NC_008596.1.
DR PDB; 8E9G; EM; 2.60 A; C=1-238.
DR PDB; 8E9H; EM; 2.70 A; C=1-238.
DR PDB; 8E9I; EM; 2.80 A; C=1-238.
DR PDBsum; 8E9G; -.
DR PDBsum; 8E9H; -.
DR PDBsum; 8E9I; -.
DR AlphaFoldDB; A0QU34; -.
DR EMDB; EMD-27963; -.
DR EMDB; EMD-27964; -.
DR EMDB; EMD-27965; -.
DR SMR; A0QU34; -.
DR STRING; 246196.MSMEG_2061; -.
DR PaxDb; 246196-MSMEI_2016; -.
DR GeneID; 66733489; -.
DR KEGG; msg:MSMEI_2016; -.
DR KEGG; msm:MSMEG_2061; -.
DR PATRIC; fig|246196.19.peg.2037; -.
DR eggNOG; COG0852; Bacteria.
DR OrthoDB; 9803286at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR NCBIfam; TIGR01961; NuoC_fam; 1.
DR PANTHER; PTHR10884:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10884; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3; 1.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; Nqo5-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; NAD; Quinone; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..238
FT /note="NADH-quinone oxidoreductase subunit C"
FT /id="PRO_0000358137"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:8E9G"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:8E9G"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:8E9G"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:8E9G"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:8E9G"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:8E9G"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:8E9H"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:8E9G"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:8E9G"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:8E9H"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:8E9G"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:8E9G"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:8E9G"
SQ SEQUENCE 238 AA; 26580 MW; 7CB55207014DD1CE CRC64;
MSTSNGSANG TNGVGLPRGD EPEIIAVRRG MFGNRDTGDT SGYGRLVRPV ALPGSTPRPY
GGYFDAVMDR LAEVLGEERY AMSIERVVVY RDQLTIEVSR VQLPAVASVL RDDPDLRFEL
CLGVSGVHYP EDTGRELHAV YPLMSITHNR RIQLEVAAPD ADPHIPSLYA VYPTTDWHER
ETYDFFGIIF DGHPSLTRIE MPDDWEGHPQ RKDYPLGGIP VEYHGAQIPP PDQRRSYS
//
