ID U5EIK4_NOCAS Unreviewed; 594 AA.
AC U5EIK4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|HAMAP-Rule:MF_01351};
DE Includes:
DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01351};
DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
DE AltName: Full=NDH-1 subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
DE Includes:
DE RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01350};
DE AltName: Full=NADH dehydrogenase I subunit H {ECO:0000256|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-1 subunit H {ECO:0000256|HAMAP-Rule:MF_01350};
GN Name=nuoI {ECO:0000256|HAMAP-Rule:MF_01351,
GN ECO:0000313|EMBL:GAD86221.1};
GN Synonyms=nuoH {ECO:0000256|HAMAP-Rule:MF_01350};
GN ORFNames=NCAST_32_07080 {ECO:0000313|EMBL:GAD86221.1};
OS Nocardia asteroides NBRC 15531.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD86221.1, ECO:0000313|Proteomes:UP000017048};
RN [1] {ECO:0000313|EMBL:GAD86221.1, ECO:0000313|Proteomes:UP000017048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD86221.1,
RC ECO:0000313|Proteomes:UP000017048};
RX PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA Suzuki K., Fujita N., Gonoi T.;
RT "Genome based analysis of type-I polyketide synthase and nonribosomal
RT peptide synthetase gene clusters in seven strains of five representative
RT Nocardia species.";
RL BMC Genomics 15:323-323(2014).
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.
CC {ECO:0000256|HAMAP-Rule:MF_01350}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_01351};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01351};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01351};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01350,
CC ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}. Cell
CC membrane {ECO:0000256|HAMAP-Rule:MF_01351}; Peripheral membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_01351}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01351}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}.
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:GAD86221.1}.
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DR EMBL; BAFO02000032; GAD86221.1; -; Genomic_DNA.
DR AlphaFoldDB; U5EIK4; -.
DR STRING; 1824.SAMN05444423_102401; -.
DR eggNOG; COG1005; Bacteria.
DR eggNOG; COG1143; Bacteria.
DR OrthoDB; 9803734at2; -.
DR Proteomes; UP000017048; Unassembled WGS sequence.
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 Gene3D; 3.30.70.3270; -; 1.
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 NCBIfam; TIGR01971; NuoI; 1.
DR PANTHER; PTHR11432; NADH DEHYDROGENASE SUBUNIT 1; 1.
DR PANTHER; PTHR11432:SF3; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 1; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF00146; NADHdh; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01351};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01351};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01351};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01351};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01351};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000256|RuleBase:RU000471};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
KW Reference proteome {ECO:0000313|Proteomes:UP000017048};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01350};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01350}; Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 327..349
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01350"
FT DOMAIN 461..492
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 508..537
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 472
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 475
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 478
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 482
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 517
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 520
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 523
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT BINDING 527
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
SQ SEQUENCE 594 AA; 65019 MW; 6356085FD1D886D6 CRC64;
MSDPVLLLAA DAAPVFGTDP LWLVVLKALG VFVYLMLVPL IAVLAERKVV ARMQMRLGPN
RVGPGGIFQS IADGVKMALK EDIVPAIVDK PIFVLAPIIS VIPAFMAFAV IPFGPEVSIF
GQTTALQLTD MPVGVLYILA ITSIGVYGIV LAGWSSGSTY PLLGGLRSTA QVISYEIAMA
LTFATVFLLS GTMATSGIVS AQEGTWYVFL LLPSFLIYCV AMVGETNRAP FDLPEAEGEL
VGGFHTEYSS LKFAMFMLAE YVNMATVSAL ATTLFLGGWR APFPINLWEG ANSGWWPLLW
FTLKVWTFLF VFVWLRGTLP RLRYDQFMNL GWKLLIPTSL VWVMIVAGAR VLDIEGIPGQ
TAILVTVGIL ITAWMIWTFL RAGRAEGLPP LPEAPAKSPV FLGFPTPPMP PRPAGEKAEL
GLFEPLAGFA VTAATMFKKP NTESYPEQKV PTAPRYHGRH QLNRYDDGLE KCIGCELCAW
ACPADAIFVE GADNTEDERF SPGERYGRVY QINYLRCIGC GLCIEACPTR ALTMTNEYEL
TDDNRADLIY EKDRLLAPLQ DGMTAPPHAM APGTDEADYY LGRVRPTTSE EVLR
//
