ID A0A1B8FU12_9PEZI Unreviewed; 509 AA.
AC A0A1B8FU12;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-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=VE02_05009 {ECO:0000313|EMBL:OBT87075.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT87075.1};
RN [1] {ECO:0000313|EMBL:OBT87075.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT87075.1};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KV459409; OBT87075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8FU12; -.
DR Proteomes; UP000091872; 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 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 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 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:OBT87075.1}.
FT DOMAIN 392..437
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 55300 MW; 0062B82BA90EDC2D CRC64;
MLSRNATSPA LTSIASRVLP GAASAGARLG GPGASAAQQQ TRGLATVQDA PAPKRIYGGL
RDQDRIFQNL YSHHGPDLAS AKKYGDWHKT KEILDKGHDW IISEVKASGL RGRGGAGFPS
GLKWSFMNFK GWENDNKPRY LVVNADEGEP GTCKDREIMR KDPHKLLEGC LVAGRAMNCS
AAYIYIRGEF IHEAAVLQNA IQEAYKDGLI GKNACNSGYD FDIYLHRGMG AYVCGEETSL
IESLEGKPGK PRLKPPFPAS VGLFGCPSTV ANVETIAVAP TICRRGGDWF AGFGRERNAG
TKLFCISGHV NNPCTVEEEM SIPLRELIDK HCGGVRGGWD NLKAVIPGGS STPILPKSVC
DDQIMDFDGL KDSQSGLGTA AVIVMDKSTD VVRAISRLSH FYRHESCGQC TPCREGSKWT
EQIMQRFEKG QGREREIDML QELTKQVEGH TICALGEAFA WPIQGLIRHF RPELEARMQK
FAEENGGAAL AGGWQHDSKA QGKLVAPGQ
//
