ID A0A256B8C1_9CYAN Unreviewed; 507 AA.
AC A0A256B8C1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=NAD(P)H-quinone oxidoreductase subunit D4 {ECO:0000313|EMBL:OYQ61905.1};
GN ORFNames=B9G53_25290 {ECO:0000313|EMBL:OYQ61905.1};
OS Pseudanabaena sp. SR411.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=1980935 {ECO:0000313|EMBL:OYQ61905.1, ECO:0000313|Proteomes:UP000215660};
RN [1] {ECO:0000313|EMBL:OYQ61905.1, ECO:0000313|Proteomes:UP000215660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR411 {ECO:0000313|EMBL:OYQ61905.1,
RC ECO:0000313|Proteomes:UP000215660};
RA Stowe E.L., Hundermark E.L., Stowe W.;
RT "Novel uncharacterized cyanobacterium from Susquehanna River.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, 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 believed
CC to be plastoquinone. Couples the redox reaction to proton translocation
CC (for every two electrons transferred, four hydrogen ions are
CC translocated across the cytoplasmic membrane), and thus conserves the
CC redox energy in a proton gradient. {ECO:0000256|ARBA:ARBA00025624}.
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 4 family.
CC {ECO:0000256|ARBA:ARBA00009025}.
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:OYQ61905.1}.
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DR EMBL; NDHW01000245; OYQ61905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256B8C1; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000215660; 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 InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR NCBIfam; TIGR01972; NDH_I_M; 1.
DR PANTHER; PTHR43507:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE CHAIN 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000215660};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..422
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 507 AA; 54710 MW; BB22D2CE19C778E0 CRC64;
MLSTLVWVPI AGALLIVLLG AFLDFQQLRR ISLGIAIATF GWSIFLLTKF DISLASIQLS
ESFAWLDPIG LTYRLGVDGL SFPLVLLNGL LLIIAIYISY DIQRPRLYFP LILLLGGGVN
GAFLAQNLLL FFLLFEVELI PLYLLIAIWG GEKRGYAATK FLIYTAISGV LILAAFFGMA
VFGSGDAATF TFNYQDLHLE GVSKTTKGIL LLLLLLGFGI KIPIVPLHTW LPDAHVEAST
PVSTLLAGVL LKLGTYGLLR FGLGLLPDAW QAIAPFLAVW AVVSVIYGCL TAITQTDMKK
MVAYSSVGHM GYILLALAAA TPLSLVGATF QMISHGLISA LLFILVGIVY KKTGTRNINS
LNGLLNPERG LPITGSLMIL AAMASAGTPG MIGFIAEFVI FRSSFAVFPV QTLLCMIGTG
LTAVYFLIMI DRVFFGRLAV EKIANKPPIS NFPFAKWQEK FPAIALALII VFFGLIPSFA
TKIIESSADA IAPNHTKPSQ IALVQSI
//
