ID V6H9E0_9LEPT Unreviewed; 484 AA.
AC V6H9E0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=NADH-ubiquinone oxidoreductase-G iron-sulfur binding region {ECO:0000313|EMBL:EQA34748.1};
GN ORFNames=LEP1GSC047_1337 {ECO:0000313|EMBL:EQA34748.1};
OS Leptospira inadai serovar Lyme str. 10.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049790 {ECO:0000313|EMBL:EQA34748.1, ECO:0000313|Proteomes:UP000018719};
RN [1] {ECO:0000313|EMBL:EQA34748.1, ECO:0000313|Proteomes:UP000018719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10 {ECO:0000313|EMBL:EQA34748.1,
RC ECO:0000313|Proteomes:UP000018719};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAY-2013) 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 -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
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:EQA34748.1}.
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DR EMBL; AHMM02000025; EQA34748.1; -; Genomic_DNA.
DR RefSeq; WP_010416759.1; NZ_AHMM02000025.1.
DR AlphaFoldDB; V6H9E0; -.
DR STRING; 1049790.LEP1GSC047_1337; -.
DR Proteomes; UP000018719; 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: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; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
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:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; 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; PS00643; COMPLEX1_75K_3; 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:ARBA00022485};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Ubiquinone {ECO:0000313|EMBL:EQA34748.1}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 215..271
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 484 AA; 53830 MW; B13A095C7C53FD3A CRC64;
MVKIKIDGIE YEVDEKKNLI SAAKDVGVDI PFFCFHPKLS VVGMCRMCLI EIEGIPRLQV
ACNTKVTEGL SIVTNSPRVK EAREGTMEFL LANHPLDCPV CDKAGECQLQ DNSFKEGKGN
SRFTLEKRNI PQEEIGTNLI INHNRCIVCY RCVRFEEELV GESNLGLFER GYHSIIGLAK
EEPIAHNYQG ALADICPVGA LLNNKTLFKS RVWWYKSEES ICPGCSTGCK TYSNVRDNKM
YRYMPRIDEE KDQYFLCDKG RFDVDWLNHN RLFAYYMDGN PSTSAQVLDT IALKVSQASG
VAILGGAHES DQNLQSIKKS LEKVGIPIAT EARVSAAQYK DPEQIDFQYT TDAHPNTKGA
VDADFISASG LESLLSSISK GEYDVVFLIK ENVSDVLGRV KPKTLIVLET NLSEGISHAN
FGIPIKTFAE QTGSFTNKKG WSQTFNKSME PPKGLLSSGE FFSELVARVV ELRSGQKEAA
IGDR
//
