ID A3K1E8_9RHOB Unreviewed; 730 AA.
AC A3K1E8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:EBA08744.1};
GN ORFNames=SSE37_03840 {ECO:0000313|EMBL:EBA08744.1};
OS Sagittula stellata E-37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sagittula.
OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08744.1, ECO:0000313|Proteomes:UP000005713};
RN [1] {ECO:0000313|EMBL:EBA08744.1, ECO:0000313|Proteomes:UP000005713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-37 {ECO:0000313|EMBL:EBA08744.1,
RC ECO:0000313|Proteomes:UP000005713};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
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 -!- 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:EBA08744.1}.
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DR EMBL; AAYA01000004; EBA08744.1; -; Genomic_DNA.
DR RefSeq; WP_005857512.1; NZ_AAYA01000004.1.
DR AlphaFoldDB; A3K1E8; -.
DR eggNOG; COG1009; Bacteria.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000005713; Unassembled WGS sequence.
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:UP000005713};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..109
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 136..441
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT REGION 550..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 79936 MW; A98F4B19CAEC326D CRC64;
MESIILFAPL AGALIAGFGW KFIGIRGSQW ITTGLLFLAC FFSWITFLTH GPETEHVQIL
RWIESGTLST DWSIRLDRLT SIMLIVVTTV SSLVHLYSFG YMAHDENFRE GEESYKPRFF
AYLSFFTFAM LMLVTSDNLV QMFFGWEGVG VASYLLIGFY YRKPSANAAA IKAFVVNRVG
DFGFALGIFA LFFLTDSVRF DDIFAAAPTL AETQITFLWG SWNAAEVCAF LLFIGAMGKS
AQLFLHTWLP DAMEGPTPVS ALIHAATMVT AGVFLVCRMS PLMEYAPHAM AFVTFLGATT
AFFAATVGLV QNDIKRVIAY STCSQLGYMF VAAGVGVYSV AMFHLFTHAF FKAMLFLGAG
SVIHGMHHEQ DMRNYGGLRK KLPYTFWAMM IGTLAITGVG IPLTHIGFAG FLSKDAVIES
AWAGTAGGYA FWMLVIAALF TAFYSWRLIF MTFFGKPRGN KHTHEHAHES PTVMLIPLGV
LALGAIFSGM VWYGSFFGDH ARVNAFFGIP AHHEEVAHGD DAHAEDVAEL QGAADAVNEA
EHAGEAVADE AHGEDAAATE GEGDATHAAA EGDHGSAGMA PQGAIFMAAD NTVMEDAHHA
PVWVRVSPFI AMLIGFLVAY WFYIVNPAMP KQLAENQRPL YLFLLNKWYF DEIYDFLFVQ
PAKKLGRILW KGGDEAIIKG GINGLAMGIV PWVTRLAGRA QSGYIFTYAF AMVIGIAVLI
TWMTISGGAQ
//
