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Database: UniProt
Entry: A6TVG3_ALKMQ
LinkDB: A6TVG3_ALKMQ
Original site: A6TVG3_ALKMQ 
ID   A6TVG3_ALKMQ            Unreviewed;       598 AA.
AC   A6TVG3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ABR50181.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ABR50181.1};
GN   OrderedLocusNames=Amet_4100 {ECO:0000313|EMBL:ABR50181.1};
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR50181.1, ECO:0000313|Proteomes:UP000001572};
RN   [1] {ECO:0000313|Proteomes:UP000001572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX   PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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DR   EMBL; CP000724; ABR50181.1; -; Genomic_DNA.
DR   RefSeq; WP_012065129.1; NC_009633.1.
DR   AlphaFoldDB; A6TVG3; -.
DR   STRING; 293826.Amet_4100; -.
DR   KEGG; amt:Amet_4100; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_3_2_9; -.
DR   OMA; VATFYHH; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000001572; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; cd02980; TRX_Fd_family; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
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; 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:SF3; HYDROGENASE SUBUNIT; 1.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF00037; Fer4; 2.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
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:ABR50181.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          540..569
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          571..598
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   598 AA;  64814 MW;  45232F28C53A4901 CRC64;
     MDLFRSHVLV CGGTGCASSD SFKMIDEFDE AFKKYGLEKE VKLVKTGCFG LCEAGPIVIV
     YPEGAFYSHV KLSDIDRITE EHLLKGRIVT DLLYKESYVG DQIKAIDEVG FYKKQTRIAL
     RNCGVINPEV IEEYIAYDGY KALGKVLTEM QPEEVVDIMK RSGLRGRGGG GFPAGLKWEF
     TAKAEGDEKY VACNADEGDP GAFMDRSVLE GDPHVVIEAM AIAAYAAGAN RGYVYIRAEY
     PIAVERLEIA IGQARENGLL GKDIFGTGFD FELEIRLGAG AFVCGEETAL INSIEGKRGM
     PRPRPPFPAQ KGIWNKPTLL NNVETYANVP RIILNGAEWF ASIGTEKSKG TKVFALGGKI
     NNTGLVEIAM GTTLKEVIYD IGGGIPDGKA FKAVQTGGPS GGCITAEHLD TPIDYDNLIE
     LGSMMGSGGM IVMDEDNCMV DIARFFLDFT VEESCGKCTP CREGTKRMLE LLDIISEGKG
     TVADLDKLES LAKTIKSSSL CGLGQTAPNP VLSTLKYFRD EYDAHVHDKS CPAGVCKALA
     KYLVVSELCK KCGICAKKCP VDCISGVKGK EVYLIDQEKC IKCGACLEAC PFKAIVKK
//
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