NU1C_THEVB
ID NU1C_THEVB Reviewed; 372 AA.
AC Q8DL32;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=tlr0667;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC08218.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000039; BAC08218.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_681456.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; A=1-372.
DR PDB; 6KHI; EM; 3.00 A; A=1-372.
DR PDB; 6KHJ; EM; 3.00 A; A=1-372.
DR PDB; 6L7O; EM; 3.20 A; A=1-372.
DR PDB; 6L7P; EM; 3.60 A; A=1-372.
DR PDB; 6NBX; EM; 3.50 A; A=1-372.
DR PDB; 6NBY; EM; 3.10 A; A=1-372.
DR PDB; 6TJV; EM; 3.20 A; A=1-372.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DL32; -.
DR SMR; Q8DL32; -.
DR IntAct; Q8DL32; 1.
DR STRING; 197221.22294388; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08218; BAC08218; BAC08218.
DR KEGG; tel:tlr0667; -.
DR PATRIC; fig|197221.4.peg.706; -.
DR eggNOG; COG1005; Bacteria.
DR OMA; WSGWASN; -.
DR OrthoDB; 1559067at2; -.
DR Proteomes; UP000000440; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..372
FT /note="NAD(P)H-quinone oxidoreductase subunit 1"
FT /id="PRO_0000240042"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 65..85
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 347..367
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 31..59
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6L7O"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6NBY"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6TJV"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6TJV"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6NBY"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6NBY"
FT HELIX 252..275
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 276..280
FT /evidence="ECO:0007829|PDB:6NBY"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6TJV"
FT HELIX 300..329
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 348..365
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 372 AA; 40547 MW; D4B1D0A297170A66 CRC64;
MESGIDLQGQ FISALQSLGL SHDLAKLLWL PLPMLMMLIV ATVGVLVAVW LERKISAAVQ
QRIGPEYIGP LGILAPLADG LKLIFKEDVL PANSDRWLFT LGPAVVVIPV FLSYIIVPFG
QNLLISNLAM GVFLWIALSS IAPIGLLMAG YASNNKYSLL GGLRAAAQSI SYEIPLALAV
LAVAMMSNGL GTVEIVEQQS QYGILSWNVW RQPIGFLVFW IAALAECERL PFDLPEAEEE
LVAGYQTEYA GMKFALFYLG AYVNLVLSAL LVSVLYFGGW SFPIPLETIA NLLGVSETNP
FLQIAFAVLG ITMTLIKAYF FVFLAILLRW TVPRVRIDQL LDLGWKFLLP VGLVNLLLTA
GLKLAFPVAF GG
