ID A0A0S8CDM0_9BACT Unreviewed; 651 AA.
AC A0A0S8CDM0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Adenylylsulfate reductase {ECO:0000313|EMBL:KPK21888.1};
DE EC=1.8.99.2 {ECO:0000313|EMBL:KPK21888.1};
GN ORFNames=AMK69_20825 {ECO:0000313|EMBL:KPK21888.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK21888.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK21888.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK21888.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KPK21888.1}.
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DR EMBL; LJNR01000453; KPK21888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CDM0; -.
DR PATRIC; fig|1704023.3.peg.3136; -.
DR Proteomes; UP000051394; Unassembled WGS sequence.
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:KPK21888.1}.
FT DOMAIN 25..270
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 651 AA; 72606 MW; E3BFD8096F02659D CRC64;
MALPNKPTGE VLCKRDPEVE EREVDILIVG GGMAACGSAF EVKKWSGDKK VLLVDKAAME
RSGAVAQGLS AINTYIGENS PVDYAKMVAN DLMGITRDDL CYDLGRHVDD SVHLFEEWGL
PIWKKSAEGK NLDGKKGLEV GSLKSGAQPV RTGKWQIMIN GESYKCIVAE AAKKALGEEN
ILERVFIVKL LLDANKENTI AGAVGFSVRE NKVYVIKCKA MMVACGGAVN IYMPRAQGEG
KGRAWYPVWN SGSTYTMCAQ VGAELTMMEN RFTPARFKDG YGPVGAWFLL FKAKTLNGLG
ENYAASDFSK KELEKYAPYG LAAVTPTCLR NHLMLAEMKA GRGPIIMDTV TALAELGKSM
DAKELKHLES EAWEDFLDMT CGQANLWCAQ DCEPEKKNSE VMPTEPYLLG SHSGCCGIWV
SGPDEPWVPD HYKWGYNRMT TVNGLFTAGD GVGASGHKFS SGSHAEGRIA IKAAVKYVRD
HADFAPALKA STQELVDEVY QPVRLFLDNF KYTTAVDINP NYLKPSGFAM RLMKATNEYG
GGWMTYYQTS EKALEMLMDL FKVMHEDSMK LGAGDLHELM RCWEMRHRLW TVEAHCRHIQ
YRKETRYPGF YYNADHPGQD DENWFCFTNS KYDPKTGQWE CKKVPHVKIF K
//
