ID A3PBW8_PROM0 Unreviewed; 513 AA.
AC A3PBW8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Putative NADH Dehydrogenase (Complex I) subunit (Chain 4) {ECO:0000313|EMBL:ABO17243.1};
DE EC=1.6.5.3 {ECO:0000313|EMBL:ABO17243.1};
GN OrderedLocusNames=P9301_06201 {ECO:0000313|EMBL:ABO17243.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17243.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO17243.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17243.1,
RC ECO:0000313|Proteomes:UP000001430};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000576; ABO17243.1; -; Genomic_DNA.
DR RefSeq; WP_011862610.1; NC_009091.1.
DR AlphaFoldDB; A3PBW8; -.
DR STRING; 167546.P9301_06201; -.
DR KEGG; pmg:P9301_06201; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_4_3; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000001430; Chromosome.
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 Oxidoreductase {ECO:0000313|EMBL:ABO17243.1};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..419
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 513 AA; 55304 MW; E079E1E86DC43CE8 CRC64;
MNLESFPWLS SVVLLPLIGA IIMPFLSSKE GEDNTLPRNI SLSFLFIDFL LIIGVLFQKF
NTSDSSLQLV ERASWLPSIG LEWSLGVDGL SAPLVALSGL ITFLSAAASW KIKKKSNLYF
ALLLVQASAQ ALVFLSQDFL LFFLAWELEL VPVYLLIAIW GGKKKLYAAT KFILYTALAS
LLILISGLAL ALSGDTFTLN ITDITNKHVT GSLALLSYLG FLIGFGVKLP IFPLHTWLPD
AHGEANAPVS MLLAGILLKM GGYALLRFNV QILPEVHLQI APALIILGII NIIYGALNAF
AQDNVKRRIA CSSVSHMGFV LLGIGAVDAL GISGAMLQMI SHGLIAAAMF FVTGSFYERT
NTLSIPNMGG LAKVLPITFA FFLASSLASL ALPGMSGFIS EITVFLGITS QEGFSSIFRS
ITILIAAIGL VLTPIYLLSM CRRVFFGPRI PALATVKEMN GRELTIGFSL LLPTLVIGFW
PKIAINLYES STNALSQQLT LAKLVGLIPT LVN
//
