ID A0A7S9A2H1_9TREE Unreviewed; 506 AA. AC A0A7S9A2H1; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 24-JAN-2024, entry version 7. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|ARBA:ARBA00021008}; DE AltName: Full=NADH dehydrogenase subunit 2 {ECO:0000256|ARBA:ARBA00031028}; GN Name=nad2 {ECO:0000313|EMBL:QPF23699.1}; OS Trichosporon inkin. OG Mitochondrion {ECO:0000313|EMBL:QPF23699.1}. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Trichosporonales; Trichosporonaceae; Trichosporon. OX NCBI_TaxID=82517 {ECO:0000313|EMBL:QPF23699.1}; RN [1] {ECO:0000313|EMBL:QPF23699.1} RP NUCLEOTIDE SEQUENCE. RA Liu Q.; RT "Characterization and phylogenetic analysis of the complete mitochondrial RT genome of opportunistic pathogen Trichosporon sp. (Trichosporonales: RT Trichosporonaceae)."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|ARBA:ARBA00003257}. 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|ARBA:ARBA00000766}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007012}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MT801082; QPF23699.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7S9A2H1; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR HAMAP; MF_00445; NDH1_NuoN_1; 1. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; ND/Mrp_mem. DR NCBIfam; TIGR01770; NDH_I_N; 1. DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1. DR PANTHER; PTHR22773:SF41; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1. DR Pfam; PF00361; Proton_antipo_M; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022660}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000313|EMBL:QPF23699.1}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022660}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..506 FT /note="NADH-ubiquinone oxidoreductase chain 2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030992111" FT TRANSMEM 20..39 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 59..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 131..150 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 162..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 201..221 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 242..262 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 282..303 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 310..328 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 340..365 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 386..409 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 421..447 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 468..487 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 125..436 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 506 AA; 55579 MW; 3A74EC5861F56F05 CRC64; MVILGIFLLM TMVALPRAKI TSTLLIRVTS ILLLFVARLS YQNRYINGMG SGLSLFNGLF NTTSITGSFD RFMAIVGAII LIGWAPRSFK KLAETQTVFT RVPTIPAYAL IILFTTCGAS FLISSSNLVS VYLRIELQSF AVYILAALYR DSESATSAGL KYFLLGGLSS GLILLGARLI YSNTGLTDLE SIFTLLSVDN NSSILLPSVI GLIIMTCGFL FKIGAAPFHN WAPDVYDGTP TIVTTWLTIM PKISILVFLL GLQRGLGNSL TVVLGNVSID VWKNLLLLCS LLSLIIGTVV GLAQYRIKRL FPYSTISHVG FLLLALGINT EESIESFLFY LIQYTITNLD AFLVLLAFGY VINYSKSFMD IHFISDLKGQ FRANPLLGLT LTICLFSMAG VPPLIGFFGK QMILYSATHS GYYFLSLVAI LLSVISASYY LNIIRVIHFE SLNKSNETLV SSNEPKITNV HSFAIATLTM VIALYMFKPS ILLNSTTLLA LTLYTF //