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Database: UniProt
Entry: L0GWL3_9GAMM
LinkDB: L0GWL3_9GAMM
Original site: L0GWL3_9GAMM 
ID   L0GWL3_9GAMM            Unreviewed;       367 AA.
AC   L0GWL3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=NADH:ubiquinone oxidoreductase 49 kD subunit 7 {ECO:0000313|EMBL:AGA91148.1};
GN   ORFNames=Thimo_2412 {ECO:0000313|EMBL:AGA91148.1};
OS   Thioflavicoccus mobilis 8321.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thioflavicoccus.
OX   NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA91148.1, ECO:0000313|Proteomes:UP000010816};
RN   [1] {ECO:0000313|EMBL:AGA91148.1, ECO:0000313|Proteomes:UP000010816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8321 {ECO:0000313|EMBL:AGA91148.1,
RC   ECO:0000313|Proteomes:UP000010816};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA   Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|RuleBase:RU003685}.
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DR   EMBL; CP003051; AGA91148.1; -; Genomic_DNA.
DR   RefSeq; WP_015281281.1; NC_019940.1.
DR   AlphaFoldDB; L0GWL3; -.
DR   STRING; 765912.Thimo_2412; -.
DR   KEGG; tmb:Thimo_2412; -.
DR   PATRIC; fig|765912.4.peg.2363; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_6; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000010816; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 2.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003685};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685};
KW   Ubiquinone {ECO:0000313|EMBL:AGA91148.1}.
FT   DOMAIN          120..285
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          290..367
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   367 AA;  41249 MW;  DF4D5D3ED8BCAC25 CRC64;
     MTDTIKIFHG PQHPGVTGNM SLELDLDGET IVAAKTHVGY LHRGFEKLIE RRTVIQAFTI
     VCRICVPEPD PNEENFARGV EELLGLEISE RAKYIRVMVL ELARLQAHYL WLAGQGGSIG
     HGVVPQWAVG ERDYILDLFE ELTGGRVYHM YIYPGGVKRD LPAGFLERLC DLVDDLERRL
     PEYDRIFFDN TAVKKRLQGV GVVDPDEALR HGYAGPVIRA CGLPRDVRRD APYLVYDQLE
     FDIPTETAGD AYARALVRRA EMYQSLRILR QVAERMPADG PIQCKLPSHR KLKLPKAETY
     VQSESARGAF GYFMAGDGSE RLRRLQVRGP SLVHAFTLLE PLLIGAQLAD VALIMVSLTT
     CPPEIER
//
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