ID M1P518_DESSD Unreviewed; 672 AA.
AC M1P518;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Dissimilatory adenylylsulfate reductase alpha subunit {ECO:0000313|EMBL:AGF78573.1};
DE EC=1.8.99.2 {ECO:0000313|EMBL:AGF78573.1};
GN OrderedLocusNames=UWK_02024 {ECO:0000313|EMBL:AGF78573.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78573.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003985; AGF78573.1; -; Genomic_DNA.
DR RefSeq; WP_015404264.1; NC_020304.1.
DR AlphaFoldDB; M1P518; -.
DR SMR; M1P518; -.
DR STRING; 1167006.UWK_02024; -.
DR KEGG; dsf:UWK_02024; -.
DR PATRIC; fig|1167006.5.peg.2214; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_3_7; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0009973; F:adenylyl-sulfate reductase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AGF78573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT DOMAIN 25..269
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 672 AA; 74816 MW; F6F8AF4996452D95 CRC64;
MALPNKPNGE LKAVENPEIV EHDVDVLIVG GGMAACGTAF EIKKWASDDL KIVLCDKASM
ERSGAVAQGL SAINTYIGEN PIENYVKMVR NDLMGVVRED LIYDCGRHVD ESVKLFEEWG
LPVWKKDADG ENLDGSKPAP TLREGGTPVR TGKWQIMING ESYKCIVAEP AKAALGEENC
LERIFIVKML LDKNKPNQIA GAVGFSTREN KVHVFRCKAA LVACGGAVNI FRPRSTGEGK
GRAWYPVWNA GSTYTMCGQV GATMTMMENR FTPARFKDGY GPVGAWFLLF KAKVQNGLGE
FYANTDAVKD ELEKFMPYGA SAVTPTCLRN HLMLNELKEG RGPIYMATDV ALNAFLDERR
EAGMDEKSLK KFWKHLESEA WEDFLDMSVG QAGLWAGANV EPEKVGSEIM PTEPYLLGSH
SGCCGIWTSG PDEAWVPDVA NDSRAHKYKW GYNRMTTVDG LFTAGDGVGA SGHKFSSGAH
AEGRIVAKQL VKFCRDNADF KPELKQTAQE LADEVYAPVK LYNEHVGAST SSNVNPNFCK
PAGIMMRLMK ATDEYGGGVA TYYMTSGKLL GICMDLLKLL REDAEKMAAG DLHELLRAWE
NYHRIWCVEM HIRHIQFREE SRYPGFYYRS DFPTCDDENW KVFVNSTFNP ETQEWLCEKV
ECINIVETDP WI
//
