ID A1RWL3_THEPD Unreviewed; 567 AA.
AC A1RWL3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=NADH dehydrogenase (Ubiquinone), 30 kDa subunit {ECO:0000313|EMBL:ABL77593.1};
GN OrderedLocusNames=Tpen_0183 {ECO:0000313|EMBL:ABL77593.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL77593.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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};
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DR EMBL; CP000505; ABL77593.1; -; Genomic_DNA.
DR RefSeq; WP_011751858.1; NC_008698.1.
DR AlphaFoldDB; A1RWL3; -.
DR STRING; 368408.Tpen_0183; -.
DR EnsemblBacteria; ABL77593; ABL77593; Tpen_0183.
DR GeneID; 4600885; -.
DR KEGG; tpe:Tpen_0183; -.
DR eggNOG; arCOG01547; Archaea.
DR HOGENOM; CLU_015134_3_1_2; -.
DR OrthoDB; 43567at2157; -.
DR Proteomes; UP000000641; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
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; PF00329; Complex1_30kDa; 1.
DR Pfam; PF00346; Complex1_49kDa; 2.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR SUPFAM; SSF143243; Nqo5-like; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 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:UP000000641}.
FT DOMAIN 33..158
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 299..465
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 471..536
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT COILED 334..361
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 240
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 243
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 530
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 533
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 567 AA; 64256 MW; 2C7DE322799D1D9C CRC64;
MNNGMERLEE KIRKEIGGLL LGVEKPYPDQ LYLYVERTKL PEVCSYVYYE LGGFLSTMAG
SDERSLHGAY RLYYVFSIEE GYEDGKKPWV VVVTNIPPHD TKFSSVTPKI PAASWYEREV
RDLLGLVPEN HPDPRRLVLP DDWPEGVHPL RKEFTYTERP PSVARKCEFR PSVEGEGIMQ
VPIGPVHAVA DEPGQFRVFL DGEKVVDVDY RMFYVHRGIE KLAESRLTYN QVPFIAERIC
GICGYAHSCA YCQAVEQALG IEVPERALYI RTLMLEVERL HSHLLNLGLA CHLAGFDWGF
MAFFKAREKV MYMAELLTGG RKTYGMNVVG GVRRDITEDR AKKALEILKE VEKEYKAVLD
AVLSTSTLVS RAKDVGVLPR DVARKVSVVG PVARGSSIKR DTRKDHPYAA YSEVDFKVPV
HSEGDVLARL SVRAEETFET ISIIRQVLEN MPGGPIQAEV KEYRPYARGL GYVEAPRGED
VHFVITGPHS KVYRWRVRAS TYNNWPAIPY MCRGYTLADL PLIIGSIDPC YSCTERVIVV
DVKSGRTRVF PYEYLVSLSR KGGKPWA
//
