NUOHI_NOCFA
ID NUOHI_NOCFA Reviewed; 597 AA.
AC Q5YWD4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=NADH-quinone oxidoreductase subunits H/I;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunits H/I;
DE AltName: Full=NDH-1 subunit H/I;
GN Name=nuoH/I; OrderedLocusNames=NFA_26600;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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. This subunit may bind ubiquinone. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA,
CC H/I, J, K, L, M, N constitute the membrane sector of the complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the complex I subunit
CC 1 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the complex I 23 kDa
CC subunit family. {ECO:0000305}.
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DR EMBL; AP006618; BAD57507.1; -; Genomic_DNA.
DR RefSeq; WP_011209192.1; NC_006361.1.
DR AlphaFoldDB; Q5YWD4; -.
DR SMR; Q5YWD4; -.
DR STRING; 247156.NFA_26600; -.
DR EnsemblBacteria; BAD57507; BAD57507; NFA_26600.
DR GeneID; 61133401; -.
DR KEGG; nfa:NFA_26600; -.
DR eggNOG; COG1005; Bacteria.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_015134_8_0_11; -.
DR OMA; PNTEFYP; -.
DR BioCyc; NFAR247156:NFA_RS13310-MON; -.
DR Proteomes; UP000006820; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF00146; NADHdh; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW Quinone; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Ubiquinone.
FT CHAIN 1..597
FT /note="NADH-quinone oxidoreductase subunits H/I"
FT /id="PRO_0000246072"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 455..485
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 501..530
FT /note="4Fe-4S ferredoxin-type 2"
FT REGION 1..405
FT /note="NADH-quinone oxidoreductase subunit H"
FT REGION 406..597
FT /note="NADH-quinone oxidoreductase subunit I"
FT BINDING 465
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 597 AA; 64393 MW; 8EEFCCB584175C7F CRC64;
MPDLSLFGHD PFWLVVAKSV FLFVYIILIP LVAVLAERKV VARMQMRVGP NRVGPFGSLQ
SIADGVKMAF KEDLVPAIVD KPIYLLAPVV SVIPAFMAFA VIPLGGEVSV AGNTTALQLT
DMPVGVLYIL AITSIGVYGI VLAGWASGST YPLLGGLRST AQVISYEIAM ALCFAAVFLH
AGTMATSGIV GAQHPTWFVF LLLPSFLIYC VSMVGETNRA PFDLPEAEGE LVGGFHTEYS
SLKFAMFMLA EYVNMGTVSA LATTLFLGGW SAPWPFNLIP GADAGWWGLL WFTAKVWTFM
FVFVWLRGTL PRLRYDQFMR LGWQLLIPVS LLWVMLVATA RLLRADGHAW ATGAQVVVGV
ALTAAMIGLF LRAGRRPAAP PEPEPEPSGE AVFLGFPTPP VPADAHRVDN PKGGLLEPLA
GFAVTAATMF KKPNTEFYPE QKVPTAPRYH GRHQLNRHPD GLEKCIGCEL CAWACPADAI
YVEGADNTED ERYSPGERYG RVYQINYLRC IGCGLCIEAC PTRALTMTND YELTDDNRAD
LIYEKDRLLA PLAPGMVAPP PAMAPGTTEA DYYLGAVTGG APAAEQPAPA GAKGGAR
