ID A0A1G9G420_9RHOB Unreviewed; 514 AA.
AC A0A1G9G420;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=NADH-quinone oxidoreductase subunit M {ECO:0000313|EMBL:SDK95438.1};
GN ORFNames=SAMN05216257_10689 {ECO:0000313|EMBL:SDK95438.1};
OS Meinhardsimonia xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meinhardsimonia.
OX NCBI_TaxID=990712 {ECO:0000313|EMBL:SDK95438.1, ECO:0000313|Proteomes:UP000199328};
RN [1] {ECO:0000313|Proteomes:UP000199328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10789 {ECO:0000313|Proteomes:UP000199328};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNFV01000006; SDK95438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9G420; -.
DR STRING; 990712.SAMN05216257_10689; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000199328; 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; 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; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199328};
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..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..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 130..427
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 514 AA; 55916 MW; 234386C3D4717B85 CRC64;
MTNLLSIVTF LPLVAAAILA LFLRGEDEAA QRNAKWLALI ATTATFIASL FLLAGFDPND
TGFQFVEERD WILGLKYKMG VDGISILFVL LTTFLMPLTI AACWDVRVRV KEYMIAFLVL
ETLMIGVFTA LDLVLFYLFF EGGLIPMFLI IGIWGGKDRI YAAFKFFLYT FLGSVLMLVA
MIAMYIDAGT TDIPTLLNHQ FSSDTLSVLG FRVIGGVQTL LWLAFFASFA VKMPMWPVHT
WLPDAHVQAP TAGSVVLAAI LLKMGGYGFL RFSVPMFPVA SELLAPLVLW LSAIAVVYTS
LVALAQTDMK KLIAYSSVAH MGYVTAGIFA FNAQGLDGAI FQMLSHGFVS GALFLCVGVI
YDRMHTREID AYGGLVNRMP AYAAVFMLFT MANVGLPGTS GFVGEFLTLM GIFQVNTWVA
AVAATGVILS AAYALWLYRR VVLGDLIKES LKAITDMNAR EKAIFAPLVA MTLLLGVYPS
LVTDIIGPST QALVSQHHTA VGGPEAPATM FAHN
//
