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Database: UniProt
Entry: A0A2G3E2T3_9FIRM
LinkDB: A0A2G3E2T3_9FIRM
Original site: A0A2G3E2T3_9FIRM 
ID   A0A2G3E2T3_9FIRM        Unreviewed;       360 AA.
AC   A0A2G3E2T3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000313|EMBL:PHU37582.1};
GN   ORFNames=CSX02_07075 {ECO:0000313|EMBL:PHU37582.1};
OS   Agathobacter ruminis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Agathobacter.
OX   NCBI_TaxID=1712665 {ECO:0000313|EMBL:PHU37582.1, ECO:0000313|Proteomes:UP000224563};
RN   [1] {ECO:0000313|EMBL:PHU37582.1, ECO:0000313|Proteomes:UP000224563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JK623 {ECO:0000313|EMBL:PHU37582.1,
RC   ECO:0000313|Proteomes:UP000224563};
RA   Sheridan P.O., Walker A.W., Duncan S.H., Scott K.P., Toole P.W.O., Luis P.,
RA   Flint H.J.;
RT   "Resolving the taxonomy of Roseburia spp., Eubacterium rectale and
RT   Agathobacter spp. through phylogenomic analysis.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHU37582.1, ECO:0000313|Proteomes:UP000224563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JK623 {ECO:0000313|EMBL:PHU37582.1,
RC   ECO:0000313|Proteomes:UP000224563};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
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:PHU37582.1}.
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DR   EMBL; PDYG01000040; PHU37582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G3E2T3; -.
DR   Proteomes; UP000224563; Unassembled WGS sequence.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR43485:SF1; FORMATE HYDROGENLYASE SUBUNIT 5-RELATED; 1.
DR   PANTHER; PTHR43485; HYDROGENASE-4 COMPONENT G; 1.
DR   Pfam; PF00346; Complex1_49kDa; 2.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224563}.
FT   DOMAIN          120..282
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          287..360
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   COILED          159..186
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         65
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         68
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         68
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         354
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         357
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   360 AA;  40745 MW;  81F8F0B4A7DEBD5B CRC64;
     MGKRSVVPFG PQHPVLPEPI HLDLVLEDEK VLAAVPSIGY VHRGLESLVT KKDFQEMAYV
     AERICGICSF GHGMGYCMTI EDIMNVEVPR RADYLRTIWM EMSRLHSHLL WLGLLADGFG
     FESLFMQSWR IREGILDMFE ESTGGRVIFS VNQIGGVKKD MSKEMLANFQ KRFDEMEKEV
     RKLTRVFLDD YTVKSRLEGI GILTGEDAIR RGAAGPMARA AGIAVDMRKT GYAAYDDIDF
     EVITSDKYDS YGRCEVRIGE IFQSFDIIRQ CIRKIPDTEI NVAVKGNPPE GESIVRIEQP
     RGEAFYMSRT NGTKFLDRMR VRTPTFANLP ALTQTLQGCQ YADVPLLILT IDPCISCTER
//
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