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Database: UniProt
Entry: Q5YWD4
LinkDB: Q5YWD4
Original site: Q5YWD4 
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   10-APR-2019, entry version 103.
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-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient. This subunit may
CC       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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         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
CC       NuoA, H/I, J, K, L, M, N constitute the membrane sector of the
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I
CC       subunit 1 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 23
CC       kDa subunit family. {ECO:0000305}.
DR   EMBL; AP006618; BAD57507.1; -; Genomic_DNA.
DR   RefSeq; WP_011209192.1; NC_006361.1.
DR   ProteinModelPortal; Q5YWD4; -.
DR   SMR; Q5YWD4; -.
DR   STRING; 247156.NFA_26600; -.
DR   PRIDE; Q5YWD4; -.
DR   EnsemblBacteria; BAD57507; BAD57507; NFA_26600.
DR   KEGG; nfa:NFA_26600; -.
DR   eggNOG; ENOG4105CMZ; Bacteria.
DR   eggNOG; COG1005; LUCA.
DR   eggNOG; COG1143; LUCA.
DR   KO; K00337; -.
DR   OMA; IAMALCF; -.
DR   BioCyc; NFAR247156:NFA_RS13310-MONOMER; -.
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; Complete proteome; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; Quinone; Reference proteome; Repeat; Translocase;
KW   Transmembrane; Transmembrane helix; Ubiquinone.
FT   CHAIN         1    597       NADH-quinone oxidoreductase subunits H/I.
FT                                /FTId=PRO_0000246072.
FT   TRANSMEM     12     32       Helical. {ECO:0000255}.
FT   TRANSMEM     82    102       Helical. {ECO:0000255}.
FT   TRANSMEM    124    144       Helical. {ECO:0000255}.
FT   TRANSMEM    170    190       Helical. {ECO:0000255}.
FT   TRANSMEM    195    215       Helical. {ECO:0000255}.
FT   TRANSMEM    260    280       Helical. {ECO:0000255}.
FT   TRANSMEM    286    306       Helical. {ECO:0000255}.
FT   TRANSMEM    318    338       Helical. {ECO:0000255}.
FT   TRANSMEM    351    371       Helical. {ECO:0000255}.
FT   DOMAIN      455    485       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      501    530       4Fe-4S ferredoxin-type 2.
FT   REGION        1    405       NADH-quinone oxidoreductase subunit H.
FT   REGION      406    597       NADH-quinone oxidoreductase subunit I.
FT   METAL       465    465       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       468    468       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       471    471       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       475    475       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       510    510       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       513    513       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       516    516       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       520    520       Iron-sulfur 1 (4Fe-4S). {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
//
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