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Database: UniProt
Entry: A0A0J7I3M8_9FLAO
LinkDB: A0A0J7I3M8_9FLAO
Original site: A0A0J7I3M8_9FLAO 
ID   A0A0J7I3M8_9FLAO        Unreviewed;       452 AA.
AC   A0A0J7I3M8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=ACM40_11440 {ECO:0000313|EMBL:KMQ60411.1};
OS   Chryseobacterium sp. BLS98.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=885586 {ECO:0000313|EMBL:KMQ60411.1, ECO:0000313|Proteomes:UP000036030};
RN   [1] {ECO:0000313|EMBL:KMQ60411.1, ECO:0000313|Proteomes:UP000036030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BLS98 {ECO:0000313|EMBL:KMQ60411.1,
RC   ECO:0000313|Proteomes:UP000036030};
RA   Pipes S.E., Miller J.R., Newman J.D.;
RL   Submitted (JUN-2015) 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.
CC       {ECO:0000256|RuleBase:RU364066}.
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|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU364066};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
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:KMQ60411.1}.
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DR   EMBL; LFNF01000003; KMQ60411.1; -; Genomic_DNA.
DR   RefSeq; WP_048502952.1; NZ_LFNF01000003.1.
DR   AlphaFoldDB; A0A0J7I3M8; -.
DR   STRING; 885586.ACM40_11440; -.
DR   PATRIC; fig|885586.5.peg.2359; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000036030; Unassembled WGS sequence.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 6.10.250.1450; -; 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; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
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   NCBIfam; TIGR01959; nuoF_fam; 1.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF1; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 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   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364066};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU364066};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU364066};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364066};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364066};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364066};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW   Oxidoreductase {ECO:0000313|EMBL:KMQ60411.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066}.
FT   DOMAIN          339..384
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   452 AA;  49753 MW;  6FFD70BAA3BE7C1D CRC64;
     MSKKLLLKDA HIEGIRYFET YRKQGGYTAA EKALKMTPDE ILEEVKASGL RGRGGAGFPT
     GMKWSFLAKP EGVPRHLVVN ADESEPGTFK DRYLMEFLPH LLIEGMLISS YCLGSNTSYI
     YIRGEYSWIP DILEEAIEEA KAAGFLGKNI LGTGFDCEIY VQRGGGAYIC GEETALLESL
     EGKRGNPRLK PPFPAVKGLW ERPTVVNNVE SIAAIVPIID ITGAEYAKIG VGRSTGTKLI
     SACGNINKPG VYEIDMTITV EEFIYSDEYC GGIKDGKRLK ACIPGGSSVP IVPANLLLRT
     VNGEPRYMNY ESLADGGFAT GTMMGSGGFI VLDEDQCIVE HTMTLARFYN HESCGQCTPC
     REGTGWMYKI LKKIEKGEGK MEDIDLLWDI QRKIEGNTIC PLGDAAAWPV AAAIRHFRDE
     FEWHIKNPEL SQTQNYGLAN YADPIPAVEK NA
//
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