ID A0A0S8ENC8_9GAMM Unreviewed; 635 AA.
AC A0A0S8ENC8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Adenylylsulfate reductase {ECO:0000313|EMBL:KPK50073.1};
DE EC=1.8.99.2 {ECO:0000313|EMBL:KPK50073.1};
GN ORFNames=AMS22_12720 {ECO:0000313|EMBL:KPK50073.1};
OS Thiotrichales bacterium SG8_50.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX NCBI_TaxID=1703416 {ECO:0000313|EMBL:KPK50073.1, ECO:0000313|Proteomes:UP000051903};
RN [1] {ECO:0000313|EMBL:KPK50073.1, ECO:0000313|Proteomes:UP000051903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_50 {ECO:0000313|EMBL:KPK50073.1};
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:KPK50073.1}.
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DR EMBL; LJTW01000194; KPK50073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8ENC8; -.
DR PATRIC; fig|1703416.3.peg.1187; -.
DR Proteomes; UP000051903; 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:KPK50073.1}.
FT DOMAIN 12..241
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 499..614
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 635 AA; 71104 MW; 18C5945803252600 CRC64;
MGYKTIVEDN IDILVAGAGL GGTGAAFEAR YWGKDKKIVI AEKANIDRSG AVAQGLYAIN
CYMGTRFGEN KPEDHVRYAR IDLMGMVRED LAFDMARHVD STVHNFEDWG LPIMRNEKTG
AYLREGRWQI MIHGESYKPI VAEAAKKSAD KVYNRVCITH LLMDEAKENR IAGAVGFNVR
TGNYHVFKAK TVICGAGGAS NIFKPRSVGE GAGRVWYAPW SSGSAYGLMI GAGAKMTQME
NRIVLARFKD GYGPVGAYFL HLKTYTQNAY GEEYESKWFP DLQKLVGVEY LDPEASHRTH
RPIPTCLRNH AIINEVNAGR GPIYMVTMEA FQDPHLEEIG WHNFLGMTVG QAVLWAATDV
DPKYENPELT TSEPYVMGSH ATGCGAWVSG PEDLSPPEYF WGYNRMTTVE GLFGCGDAAG
GTPHAFSSGS FTEGRLAAKA ACKYIDDGKA EGIRVSDEQI QRRKEEIYKP LETYRVYSNE
VVAGTVNPNF INPRQGLDRL QKLMDEYCGG FGVNYMTNDK LLNIGLKKMA ILGEDLDKVA
ASDIHELLRA WELKHRFLTS ESVFQHTLFR KETRWPGYYY RGDAMKLDDK NWHVLTVSRR
DPKTGEYTME KAPLYHLVGE VEDKDLAKLK AEGHH
//
