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Database: UniProt
Entry: B7ZYZ3_MAIZE
LinkDB: B7ZYZ3_MAIZE
Original site: B7ZYZ3_MAIZE 
ID   B7ZYZ3_MAIZE            Unreviewed;       504 AA.
AC   B7ZYZ3; A0A3L6G2J2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=ZEAMMB73_Zm00001d007048 {ECO:0000313|EMBL:ONM25636.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACL53142.1};
RN   [1] {ECO:0000313|EMBL:ACL53142.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACL53142.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EMBL:ONM25636.1, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb110430_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM25636.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb110430_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb110430_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
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}.
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DR   EMBL; BT054535; ACL53142.1; -; mRNA.
DR   EMBL; CM007648; ONM25636.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7ZYZ3; -.
DR   SMR; B7ZYZ3; -.
DR   IntAct; B7ZYZ3; 4.
DR   STRING; 4577.B7ZYZ3; -.
DR   PaxDb; 4577-GRMZM2G040209_P01; -.
DR   EnsemblPlants; Zm00001eb110430_T001; Zm00001eb110430_P001; Zm00001eb110430.
DR   Gramene; Zm00001eb110430_T001; Zm00001eb110430_P001; Zm00001eb110430.
DR   eggNOG; KOG2658; Eukaryota.
DR   HOGENOM; CLU_014881_1_0_1; -.
DR   InParanoid; B7ZYZ3; -.
DR   OMA; MDEACGR; -.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; B7ZYZ3; baseline and differential.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
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   InterPro; IPR019554; Soluble_ligand-bd.
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   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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:B7ZYZ3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Respiratory chain {ECO:0000256|RuleBase:RU364066};
KW   Transit peptide {ECO:0000256|RuleBase:RU364066};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|RuleBase:RU364066};
KW   Ubiquinone {ECO:0000313|EMBL:ONM25636.1}.
FT   DOMAIN          405..450
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
FT   REGION          50..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  55196 MW;  EC8A93D4E81ED34E CRC64;
     MALRRALLRS VNFSPDSKAA IEYFYSFSRA QSACSLNGAG LCPASRSFST QAATTSSTPQ
     PPPPPPPPEK THFGGLKDED RIFTNLYGLH DPFLKGAVKR GDWYRTKDLV IKGADWIVNE
     MKKSGLRGRG GAGFPSGLKW SFMPKVSDGR PSYLVVNADE SEPGTCKDRE IMRQDPHKLL
     EGCLIAGVGM RASAAYIYIR GEYVNERLNL EKARQEAYAA GLLGKNACGS GYDFDVHIHF
     GAGAYICGEE TALLESLEGK QGKPRLKPPF PANAGLYGCP TTVTNVETVA VSPTILRRGP
     EWFASFGRKN NSGTKLYCIS GHVNKPCTVE EEMSIPLKEL LERHCGGVRG GWDNLLAVIP
     GGSSVPLLPK HICDDVLMDY DALKAVQSGL GTAAVIVMDK STDVVDAIAR LSYFYKHESC
     GQCTPCREGT PWLWMIMERL KVGDAKLEEI DMLQEVTKQI EGHTICALGD AAAWPVQGLI
     RHFRPELERR IRERAERELL AASA
//
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