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Database: UniProt
Entry: A0A059LL12_9CHLO
LinkDB: A0A059LL12_9CHLO
Original site: A0A059LL12_9CHLO 
ID   A0A059LL12_9CHLO        Unreviewed;       458 AA.
AC   A0A059LL12;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=H632_c908p0 {ECO:0000313|EMBL:KDD75042.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD75042.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD75042.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD75042.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000256|RuleBase:RU364066}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={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   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU364066}; Matrix side
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:KDD75042.1}.
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DR   EMBL; AYPS01000908; KDD75042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LL12; -.
DR   STRING; 1291522.A0A059LL12; -.
DR   OrthoDB; 5483539at2759; -.
DR   Proteomes; UP000026042; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
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:UniProtKB-EC.
DR   Gene3D; 3.10.20.600; -; 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; 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   NCBIfam; TIGR01959; nuoF_fam; 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   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   Electron transport {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   Membrane {ECO:0000256|RuleBase:RU364066};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364066};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364066};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW   Respiratory chain {ECO:0000256|RuleBase:RU364066};
KW   Transit peptide {ECO:0000256|RuleBase:RU364066};
KW   Transport {ECO:0000256|RuleBase:RU364066}.
FT   DOMAIN          361..406
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   458 AA;  50527 MW;  099EC4BDAA3464B7 CRC64;
     MLQRSARAAA RPALSCVRSF FSGHEKTSFG GLEDKDRIFT NLYGKHDPFI KGAEKRGDWY
     RTKDILVKGA DWIVDQMKKS GLRGRGGAGF PSGLKWSFMP KVSDGRPSYL VVNGDESEPG
     TCKDREIMRH DPHKLVEGCL IAGTAMRARA GYIYIRGEFV EERKAVMRAI DEAYAKGYLG
     RNACGSGIDF DLNVHWGAGA YICGEETALI ESLEGKQGKP RLKPPFPANV GLYGCPSTVT
     NVETVAVAPT ILRRGPQWFS SFGRKNNHGT KLFAISGHVN RPVTVEEEMS IPLRELIERH
     AGGVRGGWDN LLAIIPGGSS VPMLNAEQCG EVLMDFDALK ERQSGLGTAA VIVMDKSTDV
     IAAIARLSYF YKHESCGQCT PCREGTTWLY DIMSRMKKGD ARVEEIDMLW ELTKQIEGHT
     ICALGDAAAW PVQGLIRHFR PVMEQRIEQA AENIRIAA
//
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