ID A0A133VLS9_9EURY Unreviewed; 383 AA.
AC A0A133VLS9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=NADH-quinone oxidoreductase subunit D domain-containing protein {ECO:0000259|Pfam:PF00346};
GN ORFNames=AKJ52_00255 {ECO:0000313|EMBL:KXB07416.1};
OS candidate division MSBL1 archaeon SCGC-AAA382C18.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698281 {ECO:0000313|EMBL:KXB07416.1, ECO:0000313|Proteomes:UP000070404};
RN [1] {ECO:0000313|EMBL:KXB07416.1, ECO:0000313|Proteomes:UP000070404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA382C18 {ECO:0000313|EMBL:KXB07416.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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:KXB07416.1}.
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DR EMBL; LHYF01000002; KXB07416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VLS9; -.
DR Proteomes; UP000070404; 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 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:UP000070404}.
FT DOMAIN 117..285
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 286..359
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 63
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 66
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 353
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 356
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 383 AA; 43092 MW; 42054456E09F21A3 CRC64;
MSFVVPVGPQ HPALEEPEHF RITVEGEEIV DVNFRLGYMH RGIEKAFEEK NFDRALYLAE
RICGICSGIH TVASVETIEQ LADIEAPRRA KYIRTMVAEL ERVHSHLLWA GIAAHEIGFM
TLFQLVWRDR ERVMDVLEML SGNRVQYSAN KIGGVRFDVK PKHLDKITNV LNQLEEDTHH
YIDVFTSDET VIARVQGEGV LSKKKAKELS AVGPTARASG VDFDVRRDDP YCAYDEIDVD
VKVAEAGDVL ANAKVRLLET LESIRILREA VDRMPQGKIA VQPPKEFPEA QATNRVEAPR
GELVYHFKSD GGEHPFRGKV RAPTLGNIPP IVEKLKGETV AEVPIVVASI DPCFCCTERV
QVVDKDTGES KIVTKEEMRE MRE
//
