NU1C_TRIEI
ID NU1C_TRIEI Reviewed; 372 AA.
AC Q115G5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NAD(P)H dehydrogenase I subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-1 subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-A {ECO:0000255|HAMAP-Rule:MF_01350};
GN Name=ndhA {ECO:0000255|HAMAP-Rule:MF_01350}; OrderedLocusNames=Tery_1579;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC and/or the photosynthetic chain. The immediate electron acceptor for
CC the enzyme in this species is believed to be plastoquinone. Couples the
CC redox reaction to proton translocation, and thus conserves the redox
CC energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01350}.
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:0000255|HAMAP-Rule:MF_01350};
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:0000255|HAMAP-Rule:MF_01350};
CC -!- SUBUNIT: NDH-1 is composed of at least 11 different subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01350}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR EMBL; CP000393; ABG50859.1; -; Genomic_DNA.
DR RefSeq; WP_011611235.1; NC_008312.1.
DR AlphaFoldDB; Q115G5; -.
DR SMR; Q115G5; -.
DR STRING; 203124.Tery_1579; -.
DR EnsemblBacteria; ABG50859; ABG50859; Tery_1579.
DR KEGG; ter:Tery_1579; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_3; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1559067at2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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 GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
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; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..372
FT /note="NAD(P)H-quinone oxidoreductase subunit 1"
FT /id="PRO_0000298855"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 372 AA; 40780 MW; 63617CD33C487450 CRC64;
MNSGIDLQRT FIQALVDLGL SSEIAKTLWL PFPMLLMIVV ATVGVLVTVW LERKISAAAQ
QRIGPEFMGP LGTLAPLADG LKLLFKEDVV PAKADPLLFT LGPVIVAVPV FLSYLVVPFG
QNLVITDLGV AIFLWIALSS IQPIGLLMSG YASNNKYSLL GGLRAAAQSI SYEIPLALAV
LAVAMMSNSL STIDIVEQQS SYGILGWNIW RQPLGFIIFW IAVLAECERL PFDLPEAEEE
LVAGYQTEYT GMKFALYYLA SYVNLVLSSL LVAVLYLGGW ESPLPVELIS NWFGVSETTP
WLQITNATLG IIMTLLKTYL LVFIAVLLRW TLPRVRIDQL LDLGWKFLLP VALVNLLLTA
ALKLTFPFAF GG
