ID A0A0N7Z5J1_9CYAN Unreviewed; 532 AA.
AC A0A0N7Z5J1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 {ECO:0000256|HAMAP-Rule:MF_00491};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00491};
DE AltName: Full=NAD(P)H dehydrogenase I, chain 4 {ECO:0000256|HAMAP-Rule:MF_00491};
DE AltName: Full=NDH-1, chain 4 {ECO:0000256|HAMAP-Rule:MF_00491};
GN Name=ndhD {ECO:0000256|HAMAP-Rule:MF_00491};
GN ORFNames=NIES2104_56060 {ECO:0000313|EMBL:GAP99049.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP99049.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAP99049.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP99049.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
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 ECO:0000256|HAMAP-Rule:MF_00491}.
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|HAMAP-Rule:MF_00491};
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|HAMAP-Rule:MF_00491};
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_00491}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00491}. 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, ECO:0000256|HAMAP-Rule:MF_00491}.
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:GAP99049.1}.
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DR EMBL; BBWW01000001; GAP99049.1; -; Genomic_DNA.
DR RefSeq; WP_059001100.1; NZ_BBWW01000001.1.
DR AlphaFoldDB; A0A0N7Z5J1; -.
DR STRING; 1552121.NIES2104_56060; -.
DR InParanoid; A0A0N7Z5J1; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000052243; Unassembled WGS sequence.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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 HAMAP; MF_00491; NDH1_NuoM; 1.
DR InterPro; IPR022997; NADH_Q_OxRdtase_chain4.
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|HAMAP-Rule:MF_00491};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00491};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00491};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW Rule:MF_00491};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_00491};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00491};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_00491};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00491,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00491}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 114..131
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 275..294
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 375..402
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 414..435
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 463..480
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT DOMAIN 133..416
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 532 AA; 58312 MW; F73A0ED479C86455 CRC64;
MVSTSFPWLT TLILLPFAAS LLIPLIPDKQ GKTVRWYGLG VGLADLVLSI YTFWKHYDFQ
NPDFQLTESY SWIPQLGINW SLAVDGISMP LVVLAALVTT LSMLAGWKVT NKPRLFFFLM
LVMYAAQIGV FCAQDMIQFF LLWEVELVPV YILVAIWGGP KRLYAATKFI LYTALASIFI
LVGALAMAFY GDNFTFNMQE LGLKDYSLSF ELLVYAGLLI AYGVKLPIFP LHTWLPDAHG
EASAPVSMIL AGVLLKMGGY ALIRMNMEML PHAHVYFAPV LAILGIVNII YGALASFAQR
NLKRRMAYSS ISHMGFVLLG IASFTEIGMS GAVLQMVSHG LIAAALFFLA GVTYDRTHTL
NMDDMGGLAK KMPSTFALFT ICSMASLALP GMSGFVGELA IFLGFTTSDA YTSVFKTVIV
LLSAVGLIVT PIYLLSMLRE MFYGKEGKAV EKEVFLDANP RELFITAALI IPIVAIGLYP
KLITQTYDVK TVQVAQNARN AVPVIAQQMV AFPGLAAPQI SAPEPELLGM LK
//
