ID A0A1X7BMQ4_9RHOB Unreviewed; 515 AA.
AC A0A1X7BMQ4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADH-quinone oxidoreductase subunit M {ECO:0000313|EMBL:SMC10895.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:SMC10895.1};
GN Name=nuoM {ECO:0000313|EMBL:SMC10895.1};
GN ORFNames=ROA7745_00703 {ECO:0000313|EMBL:SMC10895.1};
OS Roseovarius aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=475083 {ECO:0000313|EMBL:SMC10895.1, ECO:0000313|Proteomes:UP000193224};
RN [1] {ECO:0000313|EMBL:SMC10895.1, ECO:0000313|Proteomes:UP000193224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7745 {ECO:0000313|EMBL:SMC10895.1,
RC ECO:0000313|Proteomes:UP000193224};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC {ECO:0000256|ARBA:ARBA00009025}.
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DR EMBL; FWXB01000002; SMC10895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7BMQ4; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000193224; 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 InterPro; IPR000260; NADH4_N.
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; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR PANTHER; PTHR43507:SF20; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR Pfam; PF01059; Oxidored_q5_N; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:SMC10895.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193224};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..125
FT /note="NADH:ubiquinone oxidoreductase chain 4 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01059"
FT DOMAIN 130..427
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 515 AA; 56347 MW; 928A939ED2C36147 CRC64;
MDNLLSITTF IPTIAAAILL IFLRGEDEAA QRNAKWVALI ATSLTFIVSL FILFGFDPSD
TGFQFVEEHN WLLGLKYKMG VDGISVLFVL LTTFIMPLTI AASWNVTTRV KEYMIAFLIL
ETLMLGVFMA LDLVLFYLFF EAGLIPMFLI IGIWGGKERI YASFKFFLYT FLGSVLMLVA
MVAMFADAGS TDIPTLMNHQ FGSESFSLLG IQIVGGAQTL MFIAFFASFA VKMPMWPVHT
WLPDAHVQAP TAGSVVLAAI LLKMGGYGFL RFSLPMFPIG SEVMTPLVLW MSAIAIVYTS
LVALAQEDMK KLIAYSSVAH MGYVTMGIFA ANQQGIDGAI FQMISHGFIS GALFLCVGVI
YDRMHTRDID AYGGLVNRMP AYALIFMLFT MANVGLPGTS GFVGEFLTLM GIFQVNTWVA
MVATSGVILS AAYALWLYRR VVMGDLIKES LKSITDMGRR ERAIFAPLVV MTILLGVYPA
LVTDIIGPSV EALITNYDTA LADGRAASQT AAVSH
//
