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Database: UniProt
Entry: A0A117MAF7_9CHLR
LinkDB: A0A117MAF7_9CHLR
Original site: A0A117MAF7_9CHLR 
ID   A0A117MAF7_9CHLR        Unreviewed;       594 AA.
AC   A0A117MAF7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=NAD-reducing hydrogenase subunit {ECO:0000313|EMBL:KUK93281.1};
GN   ORFNames=XE06_1039 {ECO:0000313|EMBL:KUK93281.1};
OS   Anaerolineaceae bacterium 46_22.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX   NCBI_TaxID=1635294 {ECO:0000313|EMBL:KUK93281.1, ECO:0000313|Proteomes:UP000054480};
RN   [1] {ECO:0000313|Proteomes:UP000054480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK93281.1}.
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DR   EMBL; LGHA01000118; KUK93281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117MAF7; -.
DR   PATRIC; fig|1635294.3.peg.701; -.
DR   Proteomes; UP000054480; 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   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; 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; PF01512; Complex1_51K; 1.
DR   Pfam; PF12838; Fer4_7; 1.
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; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 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   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          537..566
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          567..594
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   594 AA;  65640 MW;  A815A8ED34C3D26E CRC64;
     MAYFRSHVLV SVDPVCVEKG AYELIETLQD ELVKQGLVEE VQVLETSRIG DPETEGLDLM
     VYPEAVHYTK LTLDDVPFLV EEQFLKGRIA EQYIRETKRV IDEELSAPKT KEVRIVLKNI
     GEIDPLNIED YIARDGYMAL GKVLTEMTPE ETIQEVLDSG LRGRGGAGFP TGLKWRFIRN
     AVGEQKYMLC NADEGDPGAF ANRRVLEGDP HSVVEGMIIA AYAVGASQGY IYCRAEYPIA
     VRTMKIAIEQ ARNFGLLGDN ILGSGFSFDL EVRMGAGAFV CGEETALMAS IEGHRGEPRP
     RPPFPAQKGL WEQPSNINNV ETYSNVPQII LNGAEWFANL GYNKSTGTKT FSMAGDVKNT
     GLIEVPFGIT LREIIYDVGG GIKEDKKFKA VQTGGPMGGC LPEKLLDLHM DYEALAEAGS
     ILGSGGLVVM DEDTCMVDIA RFFMEFTQDE SCGKCTPCRI GTRRILEILT RICEGKGKPD
     DIDTLRYLCD QINENSLCGL GKGAPNPVKS TLEHFLDEYE AHIYEKRCPA KVCKSLIRFE
     IIEGLCTGCT LCARNCPVDA ISGERRQTHV IDPDICIKCG ICEQLCQYDA IEIK
//
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