ID A0A2T0TCU4_9PSEU Unreviewed; 652 AA.
AC A0A2T0TCU4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:PRY43480.1};
GN ORFNames=CLV43_103223 {ECO:0000313|EMBL:PRY43480.1};
OS Umezawaea tangerina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Umezawaea.
OX NCBI_TaxID=84725 {ECO:0000313|EMBL:PRY43480.1, ECO:0000313|Proteomes:UP000239494};
RN [1] {ECO:0000313|EMBL:PRY43480.1, ECO:0000313|Proteomes:UP000239494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44720 {ECO:0000313|EMBL:PRY43480.1,
RC ECO:0000313|Proteomes:UP000239494};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001558};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC {ECO:0000256|ARBA:ARBA00008200}.
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:PRY43480.1}.
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DR EMBL; PVTF01000003; PRY43480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0TCU4; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000239494; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01974; NDH_I_L; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF01010; Proton_antipo_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR PRINTS; PR01435; NPOXDRDTASE5.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000239494};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..135
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 154..434
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 472..551
FT /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT chloroplast chain 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01010"
SQ SEQUENCE 652 AA; 69443 MW; 3496FA555807C183 CRC64;
MLAPASGATD AVAASGLASL AWLLLALPAF GAAVLLLAGK RADKWGHLLG CATIIAAFAY
GLALFFTTLG QGAEERTSEL HLFDWIPVGA LDVEFGLRLD PLSLTFVLLI TGVGSLIHIY
SIGYMAHEEG RRKFFAYLNL FVSAMLLLVL GNGFVTLYFG WEGVGLASYL LIGWYQYKPE
AASAAKKAFL MNRVGDLGLA IAIFIMFKEL GTTTYTDVFA RVDELSSGSI LAITLLLLLG
ACGKSGQFPL QAWLPDAMAG PTPVSALIHA ATMVTAGVYL IARSNPIYNL SADGRLVVMI
IGGVTLLIGC IIGCAYDDFK KVLAYSTVSQ IGYMILAVGL GPVGYALGIM HLLTHGFFKA
GLFLGAGSVM HGMNDEGNIR RMGGLAKYMP VTFATWALGY LALIGIPPFS GFFSKDAIIA
AAFGEPGWRG YVFGGVALLG AALTAFYMTR LLILVFLGKP RWKELKTSED GREYHPHESP
WSMKIPMIVL AVGSVGAGFF LENGERLAGW LEPTLGPLQE THGALDHTMV AILSVALSLV
GVALAFLLFG RKPQPTTRPL RVSFPVRAAR ADLYGNALNE ALFARPGTWL SRALVFVDNK
GVDGLVNGTA ALLGGSSGRL RRLQTGFVRS YALSMLLGAI CVLGALLMVR FS
//
