ID A0A2A3JYN0_9RHOB Unreviewed; 516 AA.
AC A0A2A3JYN0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NADH-quinone oxidoreductase subunit M {ECO:0000313|EMBL:PBD20306.1};
GN ORFNames=CLG85_04730 {ECO:0000313|EMBL:PBD20306.1};
OS Alloyangia mangrovi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Alloyangia.
OX NCBI_TaxID=1779329 {ECO:0000313|EMBL:PBD20306.1};
RN [1] {ECO:0000313|EMBL:PBD20306.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAOS 153D {ECO:0000313|EMBL:PBD20306.1};
RA Verma A., Krishnamurthi S.;
RT "Yangia sp. SAOS 153D whole genome sequencing.";
RL Submitted (SEP-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}.
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:PBD20306.1}.
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DR EMBL; NTHN01000058; PBD20306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3JYN0; -.
DR OrthoDB; 9768329at2; -.
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 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 83..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..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..438
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 516 AA; 56377 MW; 39E89A51334D3B82 CRC64;
MANLLSIVTF LPALAALILA LFLRGGDAAA DRNAKWLAMI ATTATFVISL FILFQFDPAN
TGFQMVEEGT WIMGLKYKMG VDGISVLFVM LTTFMMPLTI LASWGVKSRV KEYMIAFLLL
ETLMLGVFMA LDLVLFYLFF EAGLIPMFLI IGIWGGKERI YASFKFFLYT FFGSVLMLVA
IVAMYADAGT LDIPSLLTHE FSTAGFSVLG IHVVGGLQTM LWLAFFASFA VKMPMWPVHT
WLPDAHVQAP TAGSVVLAAI LLKMGGYGFL RFSLPMFPVG SEVLAPLVFW MSAIAIVYTS
LVALVQEDMK KLIAYSSVAH MGYVTLGIFS ANQQGVDGAI FQMISHGFVS GALFLCVGVI
YDRMHTRKID AYGGLVNRMP AYALIFMFFT MANVGLPGTS GFIGEFLTMM GIFQVNTWVA
AVAATGVILS AAYALWLYRR VVFGDLIKES LKTIQDMNTR ERWTFAPLVV MTLWLGVYPS
AALDIIGPSV EALVNHYDTA VAAADLGGTS VAEANH
//
