ID D4H2I3_DENA2 Unreviewed; 567 AA.
AC D4H2I3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ADD67044.1};
DE Flags: Precursor;
GN OrderedLocusNames=Dacet_0240 {ECO:0000313|EMBL:ADD67044.1};
OS Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Denitrovibrio.
OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67044.1, ECO:0000313|Proteomes:UP000002012};
RN [1] {ECO:0000313|EMBL:ADD67044.1, ECO:0000313|Proteomes:UP000002012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12809 / NBRC 114555 / N2460
RC {ECO:0000313|Proteomes:UP000002012};
RX PubMed=21304711; DOI=10.4056/sigs.892105;
RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT (N2460).";
RL Stand. Genomic Sci. 2:270-279(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001968; ADD67044.1; -; Genomic_DNA.
DR RefSeq; WP_013009589.1; NC_013943.1.
DR AlphaFoldDB; D4H2I3; -.
DR STRING; 522772.Dacet_0240; -.
DR PaxDb; 522772-Dacet_0240; -.
DR KEGG; dap:Dacet_0240; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_3_0; -.
DR InParanoid; D4H2I3; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000002012; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF03486; HI0933_like; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002012}.
FT DOMAIN 140..544
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 567 AA; 61684 MW; 0B40174FBC545F71 CRC64;
MSEKKDGIGS KMLSKRDFMK VSSLTVGGAI LAAGCASTSI AATGSKPVQK WDYEADVIVI
GTGPAGLSCA AAAAENGAAV IAIDANDKIG GKGILSGGNL GIGGGTRMQK ALGFVETADI
IYEDRTVPNL RKDATMTVET VDNRKVTMGM WRKISGAEDG EGMSRAFADN SLDTWNWLDG
MGCAFVKAKK SKMSQVYRGT RYFTLTARNF VDRDNAKSGD LKSGGAGIIW PLYDRADENG
VKFMLSCKMT RIIREDNDGR VLGIEANYKG KTIYMKGKKA VFLGTGSWNG NKNLKQLFLP
WLTKYPHITG EPYVKNDGKG IEAAIQVGAS LSTDRGSDWH GWHRHPGSRW HRSGAPFGIR
GFEDPFLESE SIYVNAEGNR FMNEEIGEDN PAWVGGSKPF YFAQICATQT TDEDGPVVWI
IMDETSRQKQ KLEFKPGDNV EKFMYGKGNT LQELASAINV PAGNLTASVK RYNELVAKGK
DDDFDKQEMT AKIIQPPFHA IKWGIQKHNT LGGVTINPQA RVLDWERNPI PGLYAAGECA
GAMDLIGLAR PLVFGRIAGM TIAKEEK
//
