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Database: UniProt
Entry: U4QTJ4_9BACT
LinkDB: U4QTJ4_9BACT
Original site: U4QTJ4_9BACT 
ID   U4QTJ4_9BACT            Unreviewed;       903 AA.
AC   U4QTJ4;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=NADH dehydrogenase (Quinone), chain G {ECO:0000313|EMBL:EIJ77408.1};
GN   ORFNames=C75L2_00720061 {ECO:0000313|EMBL:EIJ77408.1};
OS   Leptospirillum sp. Group II 'C75'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1159328 {ECO:0000313|EMBL:EIJ77408.1, ECO:0000313|Proteomes:UP000016760};
RN   [1] {ECO:0000313|EMBL:EIJ77408.1, ECO:0000313|Proteomes:UP000016760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22539719; DOI=10.1126/science.1218389;
RA   Denef V.J., Banfield J.F.;
RT   "In situ evolutionary rate measurements show ecological success of recently
RT   emerged bacterial hybrids.";
RL   Science 336:462-466(2012).
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};
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DR   EMBL; JH660548; EIJ77408.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4QTJ4; -.
DR   HOGENOM; CLU_000422_4_0_0; -.
DR   Proteomes; UP000016760; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   PIRSF; PIRSF036643; FDH_alpha; 2.
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; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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}.
FT   DOMAIN          2..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          137..167
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          177..206
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          215..271
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   903 AA;  100014 MW;  B8B3A879257D690A CRC64;
     MAKVTVNGIE VEVDPSYTIL KAAEKAGISI PTFCYHPRMD PAGSCRICAV ELEDSKRVVM
     SCVTPVSDGM KVLTESPKIH DARKTNLELL LLHHPLDCPV CDCGGECPLQ NMSFAYGATE
     SRFESHRNDE PEDLKSDVLV FNANRCILCG KCVRICDEIQ DVHAIGFINR GFDTIIGPPL
     GKKLDCEFCG DCLEVCPTGA ITDHFVRYKF RPWQLEQHQT TCTNCASGCQ MHVETENESI
     VRVTSKEGLG PNEGSICVVG RFGFNHVQTP QRFDTPYMRV EHRLVPASWE ELLPELGNRL
     NAIRRKGTDR IAGLISPRVS LEDAYAFQSF FRKVLRSNMI DTGARYGFMN AALPIVEATG
     TLRPLVDHED LLKAKVILLI GTDPVAESNI TGLFLKRAAR KNRARLYVVD SEAITLSNRA
     SDHIRVNPGG ESLFVSVLSE EIVSGGNLNS EWLTRKEELF KNWNVDPGAY QRLVHDLKTA
     ETGILVTGRK IFRNEKANQS IKNMMKMIGA LGWIEREGCG ILPIPEAAND LGVLMMGATY
     EWLPGLLDAR NESSRKKWES AWGTTLSYGS GGGLGQILQG IEEGKINALI TIGENPIGHF
     PSGSKVRQIL GKLDLIVSLD MFQNELVDMA HFVLPASSSF ERVGHFVSVE GFVQKSVQTM
     AHWGESLPDW EILEKISHAM GSPMGFDSSE NLMQEILRFL PDLSPSTRNG EHFVGKTGDI
     HLVNPLAPSS LLPIPGEKIS ENASRTKIVE IPAHKANRSS VSRRYASWNE KDQPVLCEIG
     QIPGEGEFIF SMTKSLFHSG KMTLQDPNLK KIQSEGKLRI NRQTARKRKI KKGEKITLSS
     AYGRCSFTVE PSPMVSEFEL LFPEHFADSQ VLALFPPEIA LSPETGTPTI PRIRVSLSNE
     TVV
//
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