ID A0A1G0XYF7_9BACT Unreviewed; 1048 AA.
AC A0A1G0XYF7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydrogenase {ECO:0000313|EMBL:OGV38704.1};
GN ORFNames=A2020_03685 {ECO:0000313|EMBL:OGV38704.1};
OS Lentisphaerae bacterium GWF2_45_14.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798572 {ECO:0000313|EMBL:OGV38704.1, ECO:0000313|Proteomes:UP000176538};
RN [1] {ECO:0000313|EMBL:OGV38704.1, ECO:0000313|Proteomes:UP000176538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV38704.1}.
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DR EMBL; MHBG01000018; OGV38704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XYF7; -.
DR STRING; 1798572.A2020_03685; -.
DR Proteomes; UP000176538; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; 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; PF14691; Fer4_20; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
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; SSF51971; Nucleotide-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 470..515
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 1048 AA; 114347 MW; 227F4FB3213C5BFD CRC64;
MALRDWDGKK IRDEKIFDIM LCMGTSCISS GALKLKQALL DEIEKHGLQK KVKVKENACE
KHGDVSFERD RAELLETGCN GFCAAGPIVV IYPGGYFYQK VSPDDAAEII ESHIIKEVPV
ERLMYRNNGT GSPIPFYREI PFFAKQKLKV LKNKGRIAAE SIDEYIGTGG YAALSKALSM
KTQDIIAEVK ASGLRGRGGA GFSTGLKWEF CSKSKGDRKY IVCNADEGDP GAFMDRSLIE
SDPHAILEGI MIGARAIGAD TGYIYCRAEY PLALKRLEIA IQACRERGLL GKNILGTDFC
FDIFVAQGSG AFVCGEETAL LHSIEGKRGE PSPRPPFPTD KGLWGMPTVL NNVETFGNIP
MIINDGAAEF RKVGTEKSPG TKIFALTGNL NNIGLIEVPI GTSIGEIIYD IGGGIPSGKE
YKSAQIGGPS GGCIPKQHLS VPVDYETLME LGAIMGSGGL VVMDDNTCMV DVARFFLEFT
QDEACGKCAP GRIGTKRLLE ILERICAGKG EDEDLDKLVS LGEMLKKTAL CGLCKTAANP
VLSTLRYFRD EYEEHIREKR CSVGVCAGLV RAPCQSACPA GVDVPGFVSL VAEKRYAEAL
RLHRERNPFA AACARVCYHT CESRCRRASL DEPLSIRGIK RFMVDQEVTV QVPEVRENAE
NAKRKIAIIG AGPSGLSCAF FLARMGYKPK VFEAESRPGG MLVQAIPAYR LPREILAREI
RMIERLGVDI ETGKKLGSDF TIDQLKEEGY DAIFIAVGAS DSIKLGLPGE ELEGVTQALT
FLKQYNVKGS VPVGQKVVVV GGGNAAVDAS RTALRLGAEE VTLIYRRTRE QMPAYEEEVE
EAENEGVKML MLTAPVEIEG KDGKATGVKC RQMRLGEFDR TGRRKADDQG GNEFVIEADQ
IIAAVSQASS LKSYIKDIDL ELNPNNYIKA NPLTGQTSEK WIFAGGDIVT GPWSVIEAVS
AGEKAAAGID DYLTGESHAF WRQDKASDTS FDPDADPVPY PREKQPLIAV ERRRNNFDEV
ELPWSEAVAV RQAKRCLRCD YGKMPPAQ
//
