ID C8VW02_DESAS Unreviewed; 625 AA.
AC C8VW02;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Adenylylsulfate reductase, alpha subunit {ECO:0000313|EMBL:ACV64289.1};
GN OrderedLocusNames=Dtox_3577 {ECO:0000313|EMBL:ACV64289.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV64289.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV64289.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001720; ACV64289.1; -; Genomic_DNA.
DR RefSeq; WP_015758976.1; NC_013216.1.
DR AlphaFoldDB; C8VW02; -.
DR STRING; 485916.Dtox_3577; -.
DR KEGG; dae:Dtox_3577; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_3_9; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000002217; 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; 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 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.
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:UP000002217}.
FT DOMAIN 12..245
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 625 AA; 69306 MW; 6BB52C43AD5FB015 CRC64;
MPNFETVEIT TDLLLIGGGM ANCGAAVEAA YWAKKNGVKV TLVDKAAMDR SGAVAMGLSA
INQYVNYAKG VNTLKDYVEY VKKDLMGIAR DDLVYNIARH VDSTVHLFEK WGLPIWLNDD
GTYVNEGRWQ IMINGESYKI IVAEAAKNAL GTENIYERVF IVEPILDGDR IAGAIGFSTR
EEKVYVFKAK AVLAAMGGAV GVFKPRSSGE GLGRSWYPPF STGSSTYFTV MAGAEQTCQE
VRFIPIRFKD GYGPVGAWFL LFKSRATNAF GENYMETNKG VLADYAPYGD AKPIPANLRN
YLGMLDVSAG KGPLFMRTEE AIANLASKYK DDEKAFKKKM KELEAEAWED FLDMTIAQAM
LWAATNTAPE EKSSEIAAAE PYFIGSHSGA SGCWVSGPRD VAPAEYQWGY TNMTTVKGLF
AAGDASGASS HKFSSGSHAE GRIAGKSAVR FCVENPEQPN VDPAVVETLK AKILKPMEVY
EANKGFTTDD EINPNYIFPK MYMFRLQKLM DEYAGGVTAN FTTSKALLEK ALELLVFLKE
DSEKLAARSL HELMRCWENI HRTVQAEVHI HTVMFREETR FPGYYMRADL PKINNEDWKC
FCNATRNPQT GEWTMRKVPV IDLAL
//
