ID A0A3C0D9C8_9BACT Unreviewed; 361 AA. AC A0A3C0D9C8; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 08-MAY-2019, entry version 4. 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}; RN [1] {ECO:0000313|EMBL:HAH92204.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA10784 {ECO:0000313|EMBL:HAH92204.1}; RX PubMed=30148503; DOI=10.1038/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 RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. This subunit may CC bind ubiquinone. {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, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|HAMAP-Rule:MF_01350}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_01350}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01350, ECO:0000256|RuleBase:RU000471}; Multi-pass membrane CC protein {ECO:0000256|HAMAP-Rule:MF_01350, CC ECO:0000256|RuleBase:RU000471}. 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; PTHR11432; 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|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|HAMAP-Rule:MF_01350, KW ECO:0000256|RuleBase:RU000471}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01350}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01350}. FT TRANSMEM 24 51 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 98 120 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 132 154 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 175 197 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 203 225 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 265 284 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 296 318 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01350}. FT TRANSMEM 339 359 Helical. {ECO:0000256|HAMAP-Rule: FT 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 //