ID A0A890JHH5_9EUCA Unreviewed; 336 AA. AC A0A890JHH5; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-MAR-2024, entry version 9. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|ARBA:ARBA00021008, ECO:0000256|RuleBase:RU003403}; DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003403}; GN Name=nad2 {ECO:0000313|EMBL:QRH17766.1}; GN Synonyms=ND2 {ECO:0000313|EMBL:UBD09502.1}; OS Grapsus albolineatus. OG Mitochondrion {ECO:0000313|EMBL:QRH17766.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; OC Eubrachyura; Grapsoidea; Grapsidae; Grapsus. OX NCBI_TaxID=156079 {ECO:0000313|EMBL:QRH17766.1}; RN [1] {ECO:0000313|EMBL:UBD09502.1} RP NUCLEOTIDE SEQUENCE. RA Liu Q.-N., Tang B.-P., Xin Z.-Z., Liu Y.; RT "The complete mitochondrial genome of Grapsus albolineatus."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QRH17766.1} RP NUCLEOTIDE SEQUENCE. RA Sun X., Cui Y., Qu J., Wang X.; 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 -!- 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:RU003403}. 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 ECO:0000256|RuleBase:RU003403}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU003403}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU003403}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007012, ECO:0000256|RuleBase:RU003403}. 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; MT755825; QRH17766.1; -; Genomic_DNA. DR EMBL; MF198247; UBD09502.1; -; Genomic_DNA. DR AlphaFoldDB; A0A890JHH5; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro. DR InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2. DR InterPro; IPR001750; ND/Mrp_mem. DR PANTHER; PTHR46552; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1. DR PANTHER; PTHR46552:SF1; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1. DR Pfam; PF00361; Proton_antipo_M; 2. DR PRINTS; PR01436; NADHDHGNASE2. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU003403}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003403}; KW Mitochondrion {ECO:0000256|RuleBase:RU003403, ECO:0000313|EMBL:QRH17766.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU003403}; NAD {ECO:0000256|RuleBase:RU003403}; KW Respiratory chain {ECO:0000256|RuleBase:RU003403}; KW Translocase {ECO:0000256|RuleBase:RU003403}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003403}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003403}; Transport {ECO:0000256|RuleBase:RU003403}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 5..22 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 58..79 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 85..106 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 118..137 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 143..163 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 194..217 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 229..247 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 267..295 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 315..335 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 24..78 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 81..281 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 336 AA; 37675 MW; 57C09E44656FC7DC CRC64; MSFPLSYFLF FFSLVLGPII SISSTSWFGA WIGLELNALS FIPLIAMKMN PYYSESALKY FLIQALGSAL LIMSSFILIS TFEMASIFLF LALLLKLGAA PFHFWFPQVM EGLAWPQAFL LMTLQKLAPM ILLSYLITSN LVTKMTIMAA MLTAVIGALG GLNNMHLRKI IAFSSINHMS WMLMALSVGD SFWLFYFLVY TIIVLSATTT FSSLQTFTLS DLVQSERSSV FNSTLISMNF LSLGGLPPLT GFIPKWLTIQ IMADLNLFIP LFFLLVSALI TLYFYLRIII SFLIVLNPSM SFNIKSKTMS HTSPALLLSL SFNLIGLLTP FYFFIT //