ID A0A2T0Y6P1_9MICO Unreviewed; 877 AA.
AC A0A2T0Y6P1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=NADH dehydrogenase subunit G {ECO:0000313|EMBL:PRZ09694.1};
GN ORFNames=BCE75_102408 {ECO:0000313|EMBL:PRZ09694.1};
OS Isoptericola sp. CG 20/1183.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1881052 {ECO:0000313|EMBL:PRZ09694.1, ECO:0000313|Proteomes:UP000239858};
RN [1] {ECO:0000313|EMBL:PRZ09694.1, ECO:0000313|Proteomes:UP000239858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG 20 {ECO:0000313|EMBL:PRZ09694.1,
RC ECO:0000313|Proteomes:UP000239858};
RA Rubin E.;
RT "Comparative analysis of microorganisms from saline springs in Andes
RT Mountain Range, Colombia.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:PRZ09694.1}.
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DR EMBL; PVTW01000002; PRZ09694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0Y6P1; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000239858; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR43105:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 4: Predicted;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000239858}.
FT DOMAIN 19..106
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 108..147
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 288..344
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 877 AA; 91592 MW; 9F332B4FD80106EE CRC64;
MTATTDKATP GGPAGEAVET VTCTIDEVEV TVPKGTLIIR AAEQVGIEIP RFCDHPLLEP
AGACRQCLVE VAMPDREGNV RAMPKPQASC TMTVTPGMVV KTQRTSAVAD KAQEGVMELL
LMNHPLDCPV CDKGGECPLQ NQAMKNGRAT SRFADVKRTF PKPIHVSSQV LLDRERCVLC
QRCTRFSEEI AGDEFIALQE RGADQQIGRF DEQVLDFAPP CGGHGEGAPG AGPAGRSAGP
VDVPLGIAQP DTSGQPFASY FSGNTVQICP VGALTSAAYR FRSRPFDLVS TPSVAEHDAC
GAAIRIDHRR GKVMRRLAGD DPAVNEEWLT DKDRFAFTWQ SAPDRIATPL VREDGELRPA
SWVEALEIAA QGLATARDDG GVGVLPGGRL TVEDAFAWSR FARTVLRTDD VDQRARVHSV
EETAFLAHEV AGTGVGVTFA DLEAAPAVLL AGLEAEEEAG ITFLRLRKAV KAGARVFSVA
PFRSRGLARL DGTLLPTAPG TEADWLGTLA TQASGGLVPA GADRETLEDV AGALGQEGAV
VLVGERLAGA PGAYTAALRL AESTGARLAW IPRRAGERGG VEAGLLPGLL PGGRPLVDDD
ARAEAAAAWG VDVGTLPDTP GLDTDGILDA LSVGQLTGAL VGGLELADLP DPVHARRALG
AARFVVALEV RHTEATALAD VVLPVAPPVE RAGSYWNWEG RVRSFGQALE SSALPDHRVL
DALAAQLDVD LGAAEPLAAH RAIAAFGAWR GQRADAPQAG PPEPPAVAAG TAVLASWHLL
LDDGALQDGE EHLAGSAKRP VARVSAVTAA GFDVFDGDLV TVSTDRGSIT VPVAITEMVD
HVVWLPTASR GCRVHDDLGA GPGAPVRIAP AEKGDDA
//
