ID A0A0S8A2X4_9BACT Unreviewed; 630 AA.
AC A0A0S8A2X4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Adenylylsulfate reductase {ECO:0000313|EMBL:KPJ93694.1};
DE EC=1.8.99.2 {ECO:0000313|EMBL:KPJ93694.1};
GN ORFNames=AMS18_05240 {ECO:0000313|EMBL:KPJ93694.1};
OS Gemmatimonas sp. SG8_17.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703355 {ECO:0000313|EMBL:KPJ93694.1, ECO:0000313|Proteomes:UP000051607};
RN [1] {ECO:0000313|EMBL:KPJ93694.1, ECO:0000313|Proteomes:UP000051607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_17 {ECO:0000313|EMBL:KPJ93694.1};
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:KPJ93694.1}.
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DR EMBL; LJNM01000078; KPJ93694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8A2X4; -.
DR PATRIC; fig|1703355.3.peg.3649; -.
DR Proteomes; UP000051607; 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; 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.
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:KPJ93694.1}.
FT DOMAIN 12..247
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 510..626
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 630 AA; 70394 MW; 51220ABCB14D4777 CRC64;
MPNFETVTVE TDLLICGGGM AACGAAVEAA YWAKKHGLKV TVVDKAAMDR SGAVAMGLSA
INQYVDLNSG NNTLNDYIDY VRNDLMGITR EDLVASIARH VDSTVHLFEK WGLPIWKDQD
GNYVHEGRWQ LMINGESYKV IVAEAAKNAL AEAGGEYFER VFITHPLMDG DKCVGAIGFS
VRENKVYVFK AKATLVAMGG AVHVFKPRST GEGFGRSWYP PFNSGASAFF TIYAGAEMTC
QEVRFIPVRF KDAYGPVGAW FLLFKSIATN AYGGNYMQDN AAELDKWEPY GKVKPRPANI
RNWLMMLDVM EGKSPIYMQT ADAIKAIADK APDEKAAKKK LKELEAEAWE DFLDMTISQA
ILWAATNVEP ERKPSEIMAC DPYFIGSHSG ASGAWVSGPE DLQTAETKAE YFWGYPHMTT
VKGMFAAGDA SGASSHKFSS GSHAEGRIAA KGAISYIVDN NTPPKVDQKQ VDALTEEILK
PLDTFEQFKG ATTDPNINPN YIRPTQFMYR LQKIMDEYSG GVSSQFKTND KLLEKGMELL
GYLKEDAAQL AAENLHELMR CWENVHRMYQ ADAHMRSILF REETRWPGYY FRADKPNMDD
KNWLAFCNCV YKRDTGEWEM IKRPVKRITA
//
