ID F8C2J6_THEGP Unreviewed; 666 AA.
AC F8C2J6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Adenylylsulfate reductase, alpha subunit {ECO:0000313|EMBL:AEH22291.1};
GN OrderedLocusNames=TOPB45_0176 {ECO:0000313|EMBL:AEH22291.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH22291.1, ECO:0000313|Proteomes:UP000006583};
RN [1] {ECO:0000313|EMBL:AEH22291.1, ECO:0000313|Proteomes:UP000006583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH22291.1,
RC ECO:0000313|Proteomes:UP000006583};
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002829; AEH22291.1; -; Genomic_DNA.
DR RefSeq; WP_013908991.1; NC_015682.1.
DR AlphaFoldDB; F8C2J6; -.
DR STRING; 795359.TOPB45_0176; -.
DR KEGG; top:TOPB45_0176; -.
DR PATRIC; fig|795359.3.peg.177; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_3_0; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000006583; Chromosome.
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; IPR011803; AprA.
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 NCBIfam; TIGR02061; aprA; 1.
DR PANTHER; PTHR11632:SF82; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006583}.
FT DOMAIN 24..274
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 543..655
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 666 AA; 75130 MW; DAC4B32C91AF0AB7 CRC64;
MPKIWHYNPG LECAEPEIVE KETDILIVGG GMAACGAAVE AVQWAKPHGL RIILCDKAAM
ERSGAVAMGL SAINTYIGEN TPDDYVRMVR CDLMGIVRED LVFDVGRHVD DTVHCFEEWG
LPIWKKDPQT GKTLDGAEAK AKGLTLKAGA QPVRSGRWQI MINGESYKVI VAEAAKNALT
GYDKAEIIER CFIVRPLLDA NEPNRCAGAV GFSVRENKIY IIKANATLLA TGGAVNVFRP
RSIGEGKGRA WYPVWNPGTG YAMCAQIGAK LVLMENRFIP ARFKDGYGPV GAWFLLFKAR
ATNAFGEDYV AKHKDELKKF APYGEASHIG TCLRNHAMLI EMEAGRGPIY MHTEWALQEA
AEKMDKKEFK HLVAEAWEDF LDMCVTQAGL WACLNIEPEK LPSEIMPTEP YLLGSHAGCA
GAWVCGPDED WVPEEYKAPW REIGLYNRMT TVKGLFCAGD TVGASGHKFS SGSHVEGRIA
AKAMVKFCLD HKDYKPTPKE NPEELKKEIY GPWYRFEQFK TATTAYEVNP NYLIPRHIQD
RLMKLMDEYV AGCSTFYKTN KVMLERGLEL IKMLKEDMEL AAARDLHELM RAYENRHRVW
TAEAHLLHIL FREETRYPGY YYRTDFPNLD DANWRCFTLS SYNPETKEWT LETYPYVQII
PDPLGP
//