ID A0A101VU12_9PROT Unreviewed; 630 AA.
AC A0A101VU12;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Adenylylsulfate reductase subunit alpha {ECO:0000313|EMBL:KUO60733.1};
GN ORFNames=APF80_11590 {ECO:0000313|EMBL:KUO60733.1};
OS Alphaproteobacteria bacterium BRH_c36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1734406 {ECO:0000313|EMBL:KUO60733.1, ECO:0000313|Proteomes:UP000053382};
RN [1] {ECO:0000313|EMBL:KUO60733.1, ECO:0000313|Proteomes:UP000053382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c36 {ECO:0000313|EMBL:KUO60733.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO60733.1}.
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DR EMBL; LOEV01000106; KUO60733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VU12; -.
DR STRING; 1734406.APF80_11590; -.
DR Proteomes; UP000053382; Unassembled WGS sequence.
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; 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}.
FT DOMAIN 12..241
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 499..613
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 630 AA; 70563 MW; 605C59FAE6975B1B CRC64;
MAYKTVVEDD IDVLVVGGGL GGTGAAWEAR FWGQDKKIII AEKANIDRSG AVAQGLYAIN
CYMGTRWGEN NPEDHVRYAR IDLMGMVRED LLFDMARHVD STVHQFEDWG LPIMRNSKTG
AYLREGRWQI MIHGESYKPI VAEAAKKSAD KVFNRICVTH LLMDNAKENR VAGAVGFNVR
TGDYHVFKSK TVIVAAGGAS NIFKPRSVGE GAGRVWYAPW SSGSAYGLMI DAGAKMTQME
NRIVLARFKD GYGPVGAYFL HLKTYTQNGV GEEYESKWFP ELQKMVGKEY LDPEVSHRTH
RPIPTCLRNH ALISEVNAGR GPIHMVTMHA FQDPHLEEVG WENFLGMTVG QAVLWAATDV
DPKSENPELT TSEPYVMGSH ATGAGGWASG PEDVSPPEYF WGYNRMMTVE GLFGAGDAVG
GTPHAFSSGS FTEGRLAAKA ACKYIDDGKA QGIRVSDDQI EQRKKEIFAP LERYKVYRNE
IVAGTVSPSY IHPKQGLDRL QKLMDEYCGG VTVNYMTNEK LLNICLKKLN IMEEDLDCLA
AKDLHELLRA WELKHRHRTA ECVTHHTLFR KETRWPGYYY RGDAMKLDDE NWHVLTVSRR
DPKTGEYTME KAPCYHLVDK DEEKPAAAAE
//
