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Database: UniProt
Entry: M5EAG2_9FIRM
LinkDB: M5EAG2_9FIRM
Original site: M5EAG2_9FIRM 
ID   M5EAG2_9FIRM            Unreviewed;       600 AA.
AC   M5EAG2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=NADH-ubiquinone oxidoreductase chain F {ECO:0000313|EMBL:CCU77730.1};
DE            EC=1.6.5.3 {ECO:0000313|EMBL:CCU77730.1};
GN   ORFNames=HSACCH_00121 {ECO:0000313|EMBL:CCU77730.1};
OS   Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU77730.1, ECO:0000313|Proteomes:UP000012063};
RN   [1] {ECO:0000313|Proteomes:UP000012063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX   PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA   Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT   "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT   Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL   Genome Announc. 1:217-225(2013).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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:CCU77730.1}.
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DR   EMBL; CAUI01000005; CCU77730.1; -; Genomic_DNA.
DR   RefSeq; WP_005487093.1; NZ_CAUI01000005.1.
DR   AlphaFoldDB; M5EAG2; -.
DR   STRING; 1293054.HSACCH_00121; -.
DR   eggNOG; COG1894; Bacteria.
DR   InParanoid; M5EAG2; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000012063; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   CDD; cd10549; MtMvhB_like; 1.
DR   CDD; cd02980; TRX_Fd_family; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 6.10.250.1450; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   PRINTS; PR00354; 7FE8SFRDOXIN.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:CCU77730.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012063};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Ubiquinone {ECO:0000313|EMBL:CCU77730.1}.
FT   DOMAIN          543..572
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          573..600
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   600 AA;  64743 MW;  6DB1E0B85F4C3B84 CRC64;
     MKDTIYRSHV LICTGTGCVS SGAKTIKESL EEELAANDLS NEIKIVETGC HGFCEKGPIM
     IVYPEGVFYC ELESDDVAEI VEEHLLKGRT VERLLFKEPM TEKNIPSYQD IDFYKKQQRI
     ALANCGQIDP EDINEYIALG GYEAAGKALS EMEPQEVVDT VKDSGLRGRG GGGFPTGLKW
     QFAKNSESDK KYLICNADEG DPGAFMDRSI LEGDPHRIIE GMLVGAYAIG ADEGYVYVRA
     EYPLAIKRLQ KAIEDAEEYG LLGEDIFSSG FNFKLHIKKG AGAFVCGEET ALMNSIEGKR
     GMPTPRPPYP AVRGLWGKPT NINNVETYAN IPYIITEGAE NFSAIGTEGS SGTKVFALTG
     KINNTGLVEV PMGTTLNEVI FEIGGGLGEG KKFKAVQTGG PSGGCLPEDY LDLPIDYDSL
     LDAGTMMGSG GMVVMDEDSC MVDVAKFFLN FTQSESCGKC TPCREGTKRM LEILTRITEG
     EGKDGDIELL LELGEHIKST SLCGLGQSAP NPVISTIRYF RDEYEAHIHD HNCPAGACTD
     LASAYVIDEE ACIGCSKCAK VCPVDAISGE IKNPFTIDPD VCIACGACEP ECPVDAISQG
//
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