ID E4PI09_MARAH Unreviewed; 422 AA.
AC E4PI09;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Sulfide-quinone reductase {ECO:0000313|EMBL:ADP99495.1};
GN OrderedLocusNames=HP15_3731 {ECO:0000313|EMBL:ADP99495.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP99495.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP99495.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001978; ADP99495.1; -; Genomic_DNA.
DR RefSeq; WP_014578863.1; NC_017506.1.
DR AlphaFoldDB; E4PI09; -.
DR STRING; 225937.HP15_3731; -.
DR GeneID; 78558171; -.
DR KEGG; mad:HP15_3731; -.
DR PATRIC; fig|225937.3.peg.3758; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_030742_2_0_6; -.
DR Proteomes; UP000007077; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR015904; Sulphide_quinone_reductase.
DR PANTHER; PTHR10632; SULFIDE:QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10632:SF2; SULFIDE:QUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 4: Predicted;
FT DOMAIN 15..132
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 422 AA; 45627 MW; 7DC4E0EDB0A2329A CRC64;
MTSNTTTTGS VKTHTVVIVG GGAAGISVAS SIHKRDGNID IAIIEPATRH HYQPGWTMVG
GGVFRPEVTS KPMSEVMPKF VSWYQQPVTA IDQDNNQVSL ADGSSVQYKA LVLAPGLELN
WGGIDGLEEA LGSNGVTSNY REGMASYTWD MVQKLKKGRA LFSQPPMPIK CAGAPQKAMY
LSADYWLKHG VLNNVDIQFH NAGAVLFGVA DYVPALEAYV EKYGIDLNFQ STLVAVNGPA
KTAVFRSTDG DGNTEDREVS FDMLHAVPPQ RAPKLIRESA LANEAGWLDL EDDTLRHKTY
ANIFGLGDAS GTGNAKTAAA VRKQAPVVAE NLVATLRNQP LEAAYLGYGS CPLTVENGKI
VLAEFGYGGV LQPSFPKWIN DGTKATRAAW WLKAKQLPTL YWHGMLKGHE WLARPAVRSP
QK
//