ID A0A3C0D9C8_9BACT Unreviewed; 361 AA. AC A0A3C0D9C8; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 14-DEC-2022, entry version 10. DE RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01350}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01350}; DE AltName: Full=NADH dehydrogenase I subunit H {ECO:0000256|HAMAP-Rule:MF_01350}; DE AltName: Full=NDH-1 subunit H {ECO:0000256|HAMAP-Rule:MF_01350}; GN Name=nuoH {ECO:0000256|HAMAP-Rule:MF_01350}; GN ORFNames=DCL96_11005 {ECO:0000313|EMBL:HAH92204.1}; OS Prevotella sp. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=59823 {ECO:0000313|EMBL:HAH92204.1, ECO:0000313|Proteomes:UP000258952}; RN [1] {ECO:0000313|EMBL:HAH92204.1, ECO:0000313|Proteomes:UP000258952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10784 {ECO:0000313|EMBL:HAH92204.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC ubiquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. This subunit may bind ubiquinone. CC {ECO:0000256|HAMAP-Rule:MF_01350}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01350}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000256|HAMAP-Rule:MF_01350}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01350, CC ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}. CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HAH92204.1}. 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; DMGU01000060; HAH92204.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3C0D9C8; -. DR Proteomes; UP000258952; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR HAMAP; MF_01350; NDH1_NuoH; 1. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS. DR PANTHER; PTHR11432; NADH DEHYDROGENASE SUBUNIT 1; 1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01350}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01350}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01350}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01350}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01350}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01350}; Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01350}. FT TRANSMEM 24..51 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 98..120 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 132..154 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 175..197 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 203..225 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 265..284 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 296..318 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350" SQ SEQUENCE 361 AA; 40093 MW; 85B52F7ED1037629 CRC64; MFDFSIVTTF IDNLLRQTLG LGDFLSILIE CVLVGICILT AYALIAIVLI FMERKVCAYF QCRLGPMRVG PWGIFQVFAD VLKMLIKEIF AVDRADKLLY YMAPFLVIIA SVGTFSFLPW NKGAHILDFN VGVFLITAVS SIGVLGVFLA GWASNNKYSV VSAMRGAVQM ISYEMSLGLC LISAVVLTGT MQVSGIVEAQ TGAWNWLIIK GHVPAILAFL VFLVAGNAEA NRGPFDLAEA ESELTAGYHT EYSGMGFGFY YLAEYLNLFV ISGIASTVFL GGWAPLNIGI EGFDNLMNLI PGFIWFFGKT FAVVWLLMWV RWTFPRLRID QILKLEWKYL MPLSLIILIM MTVCVAFGFH G //