ID A0A1Q7TGU1_9BACT Unreviewed; 603 AA.
AC A0A1Q7TGU1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:OLD87710.1};
GN ORFNames=AUG81_08430 {ECO:0000313|EMBL:OLD87710.1};
OS Verrucomicrobia bacterium 13_1_20CM_4_54_11.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1805408 {ECO:0000313|EMBL:OLD87710.1, ECO:0000313|Proteomes:UP000185599};
RN [1] {ECO:0000313|EMBL:OLD87710.1, ECO:0000313|Proteomes:UP000185599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD87710.1}.
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DR EMBL; MNIL01000094; OLD87710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7TGU1; -.
DR Proteomes; UP000185599; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal 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}.
FT DOMAIN 10..421
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 476..586
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 603 AA; 67194 MW; 6318C770ABEB0D2C CRC64;
MADYETFQHD VLVIGAGGAG LRAAIEASAA GVSVGLICKS LLGKAHTVMA EGGIAAALAN
VDERDNWKVH FADTVRGGQY VNQWRMAELH AKEAPDRVRE LEAWGAVFDR TKDGRILQRN
FGGHKYPRLA HVGDRTGLEM IRTLQDHGVH QGIDVHMERT ILTLLKQSGR VVGALGYDRE
RGRFLVFRAK AIVLATGGIG RAYKITSNSW EYTGDGHALA YVAGAELIDM EFVQFHPTGM
VWPPSVCGIL VTEGVRGEGG ILTNKDGRRF MFDSIPENYR AQTADNEEEG WRYCQGDKDA
RRPPELLTRD HIARCIVREI KEGRGSPHGG VFLDIAWIKK KIPNAAEHIK KKLPSMYHQF
KQLADIDITE QPMEVGPTTH YVMGGIRVDS DTQMSRLPGL FAAGECAAGI NGANRLGGNS
LSDLLVFGKR AGEFAAQFAK ENQLGDINGN EIENVAHEAL RPFERSRGEN PYMLQRDLQE
TMQDNVGIVR NEAEMTSQLE YLRKLWERAS HVGVSGNREF NPGWHTALDL KNLLTVSEAV
TRAALERKES RGAQFREDYP EKNARFANVN TIIWRGEDGR MNVRLDPLPE MPDYLKQVIE
EMK
//
