ID R5E5L6_9BURK Unreviewed; 505 AA.
AC R5E5L6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:CCX87798.1};
GN ORFNames=BN548_00271 {ECO:0000313|EMBL:CCX87798.1};
OS Parasutterella excrementihominis CAG:233.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Parasutterella.
OX NCBI_TaxID=1263099 {ECO:0000313|EMBL:CCX87798.1, ECO:0000313|Proteomes:UP000018034};
RN [1] {ECO:0000313|EMBL:CCX87798.1, ECO:0000313|Proteomes:UP000018034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:233 {ECO:0000313|Proteomes:UP000018034};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCX87798.1}.
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DR EMBL; CAXE010000160; CCX87798.1; -; Genomic_DNA.
DR AlphaFoldDB; R5E5L6; -.
DR Proteomes; UP000018034; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..505
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004378367"
FT DOMAIN 30..477
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 505 AA; 54123 MW; 50F5BBC7AD1EED83 CRC64;
MYAKLTLSAA FVALAFSHNA LAADHNLSAD ILVVGAGSAG LTAAVQAAEK GKKVILLEKN
LGVGGSSQFA EGLFAVGSEW NRLRSDPLTK EEAFKTLMEK HGYVIDAAKT KDYVEGSAEN
ISWLAGHGIK FEVVRMTPWE AATWHVISDY KGTNHGAGLI KGLKDAADKA GVETKLGTPA
TELILNKEGA VVGAKAADKK GNTYTISAKA VILATGGFGD DPQKVKNWAH RDPEGWKSSV
PIGKTGDGIV MATKAGAAMG NVSFVQHLGT EGKGIKFLGN LYATSWQPSA LWVNCDGNRF
SNEDVAFSFA QAANAIYAQP HHYGWSIFDD SQVQYMMKKG VDSGIGVLVP VGQKLPNLQK
EIDDAVAVKS DGFKTADSVA QLAKELGVPE ANLQKAVEQY NKACEVGHDG EYYKEKTYLR
PLNTKKLYAI KLKAYFFSSY GGLNTNRKHQ VLDKNNKPIK GLYATGLEVS DMVGPTYSTW
SSGHAFGFAS YSGRHAALNA IDEMK
//
