ID B3EM58_CHLPB Unreviewed; 594 AA.
AC B3EM58;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ACE03436.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ACE03436.1};
GN OrderedLocusNames=Cphamn1_0472 {ECO:0000313|EMBL:ACE03436.1};
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03436.1};
RN [1] {ECO:0000313|EMBL:ACE03436.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1 {ECO:0000313|EMBL:ACE03436.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP001101; ACE03436.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EM58; -.
DR STRING; 331678.Cphamn1_0472; -.
DR KEGG; cpb:Cphamn1_0472; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_10; -.
DR OrthoDB; 9761899at2; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ACE03436.1}.
FT DOMAIN 535..564
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 567..594
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 594 AA; 63799 MW; 1888C3E1681CA778 CRC64;
MNQKPSKPLE IIVGEGTCGI AAGSKDVIDI FTELAPEAAI KSVGCAGMCH DEVMVEIIDE
KRGACLYRKV DKKNIPDLLS FHRGEGKVRQ DLLIRSSMPS VGADYLDRQT RIALRNIGQV
DPQSLDAYRE RGGYRSIEKI ITEGIKPEQV IEEVRVSGLR GRGGAGFPTA VKWGFARSAK
GEKKYLICNG DEGDPGAFMD RSLLEGDPHN ALEGMLIAAY AIGASSGYAY IRAEYPLAVE
HFRKAIDDAR KAGLLGNNIL GSSFDFDVTI KQGAGAFVCG EETALIASIE GERGMPRIRP
PFPAVKGLFG KPTIINNVES LANLPWIIEH GGAAYAEIGT EKSKGTKVFA LAGPIKRGGL
VEVPMGTTVR EVLYDIGGGS SAGRPIKAVQ LGGPSGGCIP ESLFDTPIEY EALNATGAIM
GSGGMVVMDT KSCMVDIARY FLEFTQIESC GKCTFCRIGT LRMKELLTRI CDGQGTMDDI
DTLEDIAHQV RSSSLCGLGQ TAPNPVLTTL KYFRDEYVAH VEEKRCPAGV CKGLITHTIM
QDTCTGCSIC ERYCPVDAIT GVIKKPESWV IDHDLCVNCG MCVEVCNSDA ISVA
//
