ID A0A917SA27_9ACTN Unreviewed; 447 AA.
AC A0A917SA27;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 08-OCT-2025, entry version 11.
DE RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|ARBA:ARBA00019901, ECO:0000256|RuleBase:RU364066};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN Name=nuoF {ECO:0000313|EMBL:GGL63726.1};
GN ORFNames=GCM10011575_22630 {ECO:0000313|EMBL:GGL63726.1};
OS Microlunatus endophyticus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1716077 {ECO:0000313|EMBL:GGL63726.1, ECO:0000313|Proteomes:UP000613840};
RN [1] {ECO:0000313|EMBL:GGL63726.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 4.7306 {ECO:0000313|EMBL:GGL63726.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGL63726.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 4.7306 {ECO:0000313|EMBL:GGL63726.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) 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.
CC {ECO:0000256|RuleBase:RU364066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|ARBA:ARBA00047712,
CC ECO:0000256|RuleBase:RU364066};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|RuleBase:RU364066};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU364066};
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
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:GGL63726.1}.
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DR EMBL; BMMZ01000005; GGL63726.1; -; Genomic_DNA.
DR Proteomes; UP000613840; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD 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 GO; GO:0045333; P:cellular respiration; IEA:TreeGrafter.
DR FunFam; 1.20.1440.230:FF:000001; Mitochondrial NADH dehydrogenase flavoprotein 1; 1.
DR FunFam; 3.40.50.11540:FF:000001; NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; 1.
DR FunFam; 3.10.20.600:FF:000003; NADH-quinone oxidoreductase subunit F; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR050837; ComplexI_51kDa_subunit.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR NCBIfam; TIGR01959; nuoF_fam; 1.
DR NCBIfam; NF010120; PRK13596.1; 1.
DR PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364066};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU364066};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU364066};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364066};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364066};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364066};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU364066};
KW Reference proteome {ECO:0000313|Proteomes:UP000613840};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 337..382
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 447 AA; 48630 MW; 699D928ECFC340A8 CRC64;
MTETISAEPY SPDPITPVLT ANWGDDRAWK ITNYERRGGY KALRTALQQP QGDLVQLVKD
SQLRGRGGAG FPTGNKWGFL PDNGAPRYLV VNADESEPGA CKDMPLMMAS PHTLVEGIAI
SSYAFNAHYA FIYVRGEVLH VIRRLQQAVR EAYSAGYLGR NMLGMGYDLE VIVHAGAGAY
ICGEETALLD SLEGRRGQPR LKPPFPAVAG LYGSPTVINN VESISTIPSI VAGGADWFTS
MGVDNGKGMG IFSLSGHVRN PGQIEVPLGT TLRQLLDITG GIREGHQLKF WTPGGSSSPI
FTAEHLDTPL DYDSVAKAGS MLGTRSLQIF DETTSVVRAV TRWLEFYKHE SCGKCTPCRE
GTWWLVQILK RIEAGQGQEG DVEKLLDICD NVGGKSFCAL GDAAVTPINS AIKHFRDEFE
AGYHTPAWEL FPYEKNVIYA QPAGVAQ
//
