ID A0A0E3UR62_9ANNE Unreviewed; 185 AA. AC A0A0E3UR62; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 27-MAR-2024, entry version 29. 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}; DE Flags: Fragment; GN Name=ND2 {ECO:0000313|EMBL:AKC91565.1}; OS Satchellius mammalis. OG Mitochondrion {ECO:0000313|EMBL:AKC91565.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata; OC Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae; OC Satchellius. OX NCBI_TaxID=1150272 {ECO:0000313|EMBL:AKC91565.1}; RN [1] {ECO:0000313|EMBL:AKC91565.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Nephridia {ECO:0000313|EMBL:AKC91565.1}; RX PubMed=26074907; DOI=10.3389/fmicb.2015.00529; RA Moller P., Lund M.B., Schramm A.; RT "Evolution of the tripartite symbiosis between earthworms, RT Verminephrobacter and Flexibacter-like bacteria."; RL Front. Microbiol. 6:529-529(2015). RN [2] {ECO:0000313|EMBL:AKC91565.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Nephridia {ECO:0000313|EMBL:AKC91565.1}; RA Pelicic Vladimir; RL Submitted (JAN-2015) 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: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; KP420679; AKC91565.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0E3UR62; -. 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:UniProtKB-EC. 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; 1. 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:AKC91565.1}; 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 25..44 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 50..70 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 122..145 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT TRANSMEM 166..184 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003403" FT DOMAIN 1..134 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AKC91565.1" FT NON_TER 185 FT /evidence="ECO:0000313|EMBL:AKC91565.1" SQ SEQUENCE 185 AA; 20437 MW; A7CD99573C361BC8 CRC64; IMLMAGMNAL VGGLMGMNQS QLRTIMAYSS IGHIGWMLSL LAVFKPNASI LYFMIYSMLI APLFMYMSYF NINSTKTMNK LASIKSSVPL VMTILLLSLG GLPPLTGFLP KFMTIMTLME SMKITVLLLI AGSVMNLYFY LNIAINLMIT SPTKKMMVPM NNNSDKYIII AMSGLSLGLT PLIMM //