ID A0A0T6ABX6_9BACT Unreviewed; 624 AA.
AC A0A0T6ABX6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Adenylylsulfate reductase subunit alpha, adenylylsulfate reductase, subunit A {ECO:0000313|EMBL:KRT72529.1};
DE EC=1.8.99.2 {ECO:0000313|EMBL:KRT72529.1};
GN ORFNames=XU13_C0023G0010 {ECO:0000313|EMBL:KRT72529.1};
OS Candidatus Rokubacteria bacterium CSP1-6.
OC Bacteria; Candidatus Rokubacteria.
OX NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT72529.1, ECO:0000313|Proteomes:UP000051916};
RN [1] {ECO:0000313|EMBL:KRT72529.1, ECO:0000313|Proteomes:UP000051916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT72529.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT72529.1}.
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DR EMBL; LDXP01000023; KRT72529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6ABX6; -.
DR STRING; 1640509.XU13_C0023G0010; -.
DR PATRIC; fig|1640509.3.peg.1271; -.
DR Proteomes; UP000051916; 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; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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:KRT72529.1}.
FT DOMAIN 12..244
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 504..617
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 624 AA; 69981 MW; 50C5376CEC6A24EC CRC64;
MVQPEIETVE TDVLVLGGGM AGCGAAYEAA YWAKTKGLKV AIVEKAAIER SGAVAMGLSA
INLYLGMRWN QNKPEDFVHY VRQDLMGLSR EDLVYDIARH VDSSVHLFEE WGLPIFKNAD
GTYKREGRWQ IMIHGESYKP IVAEAAKTAV GDGNVYERIF AARLLLDAKD PSKIAGAVGF
SVRENKIYVF KAKAVIVTAG GATGVFRPHS HGEGLGRIWY APWNTGSAYS MMIQAGAKMT
QMEHRLVVAR FKDGYGPVGM WFLLFKAVLK NAKGELVEQK WADLLKEWEP YGSGKPIPTP
LRNHQMMADF RAGGAPFYLM TDEAMQRMFQ EAGNDPKKIR EIEADAWEDF LDMTMSQALI
WASDNIDPAK APTEVVLTEP YLMGSHASGT GAWVSGPEDI APKEYFWGYN RMTTIKGLFA
AGDGVGGSAH KFSSGSHVEG RLAGKAAVAY ILDNGATPTV DEGQIQAIKA ELWKPFENYE
KGKSGSTKDD INPNYLFPKM ALHRLQKIMD EYAGGQGSQY ITTEHMLQKG LDRLKVFKED
LQKQAARDLH DLLRCWEVWD RTWCAEAHMR HMLFRPETRW PGYYYRADYP TLDDKNWKVF
VNSRYDASKG EWQLEKVPFL TNVS
//
