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Database: UniProt
Entry: C3MA68_SINFN
LinkDB: C3MA68_SINFN
Original site: C3MA68_SINFN 
ID   C3MA68_SINFN            Unreviewed;       664 AA.
AC   C3MA68;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=NADH dehydrogenase I chain L {ECO:0000313|EMBL:ACP24847.1};
GN   Name=nuoL {ECO:0000313|EMBL:ACP24847.1};
GN   OrderedLocusNames=NGR_c10610 {ECO:0000313|EMBL:ACP24847.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24847.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24847.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
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DR   EMBL; CP001389; ACP24847.1; -; Genomic_DNA.
DR   RefSeq; WP_012707630.1; NC_012587.1.
DR   RefSeq; YP_002825600.1; NC_012587.1.
DR   AlphaFoldDB; C3MA68; -.
DR   STRING; 394.NGR_c10610; -.
DR   KEGG; rhi:NGR_c10610; -.
DR   PATRIC; fig|394.7.peg.3883; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_6_0_5; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   Gene3D; 1.20.5.2700; -; 1.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   NCBIfam; TIGR01974; NDH_I_L; 1.
DR   PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
DR   PRINTS; PR01435; NPOXDRDTASE5.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000320};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        436..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        541..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..118
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          134..442
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   664 AA;  73539 MW;  B83F3A407ED53468 CRC64;
     MNTIIKAIVF LPLIGFLIAG LLGTQIGAKA SEYVTSGFML IALALSWFVF FDVALGHEEM
     IKVSVLRWIQ SGSFDVEWAF RVDTLTAVMF VVVNTVSTLV HIYSIGYMHH DPHRPRFFGY
     LSLFTFAMLM LITSDNLLQM FFGWEGVGLA SYLLIGFWYK KPSANAAAIK AFIVNRVGDF
     GFSLGIFSVF VLFGSINLET VFAAAQSYLP AEGAEAGEAV ITLFGMHLDK ADALTATCLL
     LFMGAMGKSA QFLLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVARMSP LFELSPDALT
     VVTLIGAITA FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV ALGVGAYGAA IFHLFTHAFF
     KALLFLGAGS VIHAVDGEQD MRYMGGLRTH IPITYWMMFI GTIALTGVGI PGTLFGTAGF
     FSKDAIIEST FASHSIVSGI AFTLLVIAAL FTSFYSWRLT FMTFHGTPRA SHEVMHHVHE
     SPQVMLVPLY ILAAGALVAG FLFHDYFFGH HYVEFWKGAL FTSAENEILE EFHHVPLWVK
     WSPFCAMALG LFTAWYMYIS RPELPKYLAD QHRGLYQFLL NKWYFDELYD FLFVRTAKRL
     GTFLWKEGDG RVIDGFGPNG VAARVLDVTD RVVRLQTGYL YHYAFVMLIG IAALVTWMML
     GSSF
//
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