ID F3QMC6_9BURK Unreviewed; 493 AA.
AC F3QMC6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Flavocytochrome c {ECO:0000313|EMBL:EGG52064.1};
GN ORFNames=HMPREF9439_02101 {ECO:0000313|EMBL:EGG52064.1};
OS Parasutterella excrementihominis YIT 11859.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Parasutterella.
OX NCBI_TaxID=762966 {ECO:0000313|EMBL:EGG52064.1, ECO:0000313|Proteomes:UP000005156};
RN [1] {ECO:0000313|EMBL:EGG52064.1, ECO:0000313|Proteomes:UP000005156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11859 {ECO:0000313|EMBL:EGG52064.1,
RC ECO:0000313|Proteomes:UP000005156};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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:EGG52064.1}.
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DR EMBL; AFBP01000075; EGG52064.1; -; Genomic_DNA.
DR RefSeq; WP_008864685.1; NZ_GL883745.1.
DR AlphaFoldDB; F3QMC6; -.
DR GeneID; 43349424; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_5_4; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000005156; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
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; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU366062};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366062};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366062}; Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 26..493
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5022269291"
FT DOMAIN 38..472
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 493 AA; 53361 MW; 53CDD1E808DCCF4D CRC64;
MEVSRRNLFK GMTVSALMMS APAFAQLEAP QKWDAEYDIV IVGGGAAGLS AATVAADEKL
SAVLFEKQSF LGGSSVLNGG MFTVAGTKEQ EKQGIKDSQE LFFKDMMRAG KNKNNPDVVK
AFVKTANEQY DFILNKLKLH PDMVVHQGYQ SVPRSHHFVT SQILTAMAAY AKKGGVKIET
GVKVLRLVWN KDHSRIAGVE IESKGKKQFV LAKKGVLLAA GGFSRNPELL GRYNPPLESA
ASIAGAGTQG DGILMGLSVG ADMLDVAYIK ATYGFRLNPK HIDEQSQLYW SGGIIVNKNV
KRFTDESQSY KVLADFALAQ PEGKSYIVFD RQMAENDFKN NPQGRILIES IVKENKVPEW
IFAGETIEDA AKKAGLNPKE LAKTVKEYNE GIKNDSDAFG RKTLVDTSGK PIPLDKGPFY
IMPATAAVIA TYCGLKINKD AKVQNVFGEV IPGLWAAGEM TGGVHGAGYM SGSAFGKAQT
FGRIAAKDIA KQK
//
