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Database: UniProt
Entry: A0A2Z6I9S7_9BURK
LinkDB: A0A2Z6I9S7_9BURK
Original site: A0A2Z6I9S7_9BURK 
ID   A0A2Z6I9S7_9BURK        Unreviewed;       472 AA.
AC   A0A2Z6I9S7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Flavocytochrome c {ECO:0000313|EMBL:BBF23139.1};
GN   ORFNames=SUTMEG_10300 {ECO:0000313|EMBL:BBF23139.1};
OS   Sutterella megalosphaeroides.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF23139.1, ECO:0000313|Proteomes:UP000271003};
RN   [1] {ECO:0000313|EMBL:BBF23139.1, ECO:0000313|Proteomes:UP000271003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF23139.1,
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; BBF23139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6I9S7; -.
DR   KEGG; sutt:SUTMEG_10300; -.
DR   OrthoDB; 9806724at2; -.
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   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.
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};
KW   Signal {ECO:0000256|RuleBase:RU366062}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT   CHAIN           20..472
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT                   /id="PRO_5022248990"
FT   DOMAIN          26..444
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   472 AA;  49248 MW;  D627848B4C163D53 CRC64;
     MKKILVAAAV ASCFGLANAA EDITVDVAVI GAGGAGLSAA VQANDLGAKV VVLEKMAMVG
     GNTIRAAGGL NATGTALQAA KGTKDSVEIM YFDTMKGGHW KNDPELVRTL CEKSASSVEW
     LLALGGDLRD VGLMAGASQA RTHRPTGGAL VGPEVIRTLY TAAKARNIDI RTNTQATEIL
     KDKSGKVIGV KVKGKDGEYT VKSKAVVNAA GGFGANNELV ASYVPRLKGF ATTNHPGATG
     DGIKMAKEAG AALIQMEEIQ THPTVVPKVG EMITEAVRGN GAVLINKDGK RFFNELDTRD
     AVSAAILKQK DGVAYLFFDS DMQKSLKATN GYIKQSYCLS GETLDEVAGK MGVDAATLKA
     TMEDWKKGKA ASKDAFGRAD MPRDLDKGPF YAILVTPAVH HTMGGIKIDS KTQVYSTKGQ
     IIPGLFAAGE ITGGVHGGNR LGGNAQADIV TFGRIAGQQA YIFAKQQDAA KK
//
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