ID A0A2Z6IA48_9BURK Unreviewed; 542 AA.
AC A0A2Z6IA48;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Flavocytochrome c {ECO:0000313|EMBL:BBF23393.1};
GN ORFNames=SUTMEG_12840 {ECO:0000313|EMBL:BBF23393.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF23393.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF23393.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF23393.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
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}.
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DR EMBL; AP018786; BBF23393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6IA48; -.
DR KEGG; sutt:SUTMEG_12840; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000271003; Chromosome.
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:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000271003}.
FT DOMAIN 79..514
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 542 AA; 57084 MW; 378CB42DF5083EA6 CRC64;
MTDEIHNTHA THESDANDLR TTRRAFCERT AKLGVGLALP AFPGLWGASA NAASAEGSES
TPVTEASHPA ESTERIEADV VVVGSGTAGL SAAVAAREAG ARRVVLLEKG AITGGHGIYS
SGSVSIARRK PEATNPAERD ADVERMVREI LEAGAGESNP ELARILAEES ESAVRWLAGM
GVEWRPLLYR AVGAVTSRNI STGTPAAGYD YVTALAGRAK TLGVRFFHST EALELLTRSG
EKASSDIKVT GVRARRKSAK EGARTVDFVA PAVVLATGGF SANVAMRMTY DARLDARYPT
TANPRGFLFD GATGDGIRMA RAVGAKEVGM RHIQVIPYSG GRLLDFVGGE IWVNDEGKRF
VSEGVPFGEL ADALHVTEGR SFWAISDAST QKSATLGVKL AEGIVREAQS IEALAAAIGV
PLSNLSATIE RWNWDARKGW DSTFERPLSG VPLTSPPFFY GRETWSVHFT CGGIAIDGKA
RVLSTRGRPI LGLYAAGETT GGLHGRDRLG GNGLTETFVF GRIAGTSAAE TASVKASLKE
AG
//
