ID A0A0M4NX64_9GAMM Unreviewed; 625 AA.
AC A0A0M4NX64;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Adenylylsulfate reductase {ECO:0000313|EMBL:ALE52552.1};
DE EC=1.8.99.2 {ECO:0000313|EMBL:ALE52552.1};
GN ORFNames=SP60_04590 {ECO:0000313|EMBL:ALE52552.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52552.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE52552.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52552.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP010552; ALE52552.1; -; Genomic_DNA.
DR RefSeq; WP_053951506.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M4NX64; -.
DR STRING; 1705394.SP60_04590; -.
DR KEGG; tho:SP60_04590; -.
DR PATRIC; fig|1705394.5.peg.918; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000058020; Chromosome.
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:ALE52552.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000058020}.
FT DOMAIN 13..245
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 502..616
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 625 AA; 70052 MW; 09A4A90A68192E03 CRC64;
MKAYKTIVED NIDILVVGAG LGGTGAAYEA RYWGRNKKIV IAEKANINRS GAVAQGLYAI
NCYMGTRFGE NNPEDHVRYA RIDLMGMVRE DLLFDMARHV DSAVHKFEEW GLPLMKDPKR
EDIGAYMREG KWQIMIHGES YKPIVAEAAT KQADKVYNRI MVTHLLMDDA QDNRVAGCVG
FNVRTGNYHV FKSKATIVGA GGASNIFKPR SVGEGAGRVW YAPWSSGSAY GLLIEAGAKM
TQMENRIVLA RFKDGYGPVG AYFLHLHTYT QNGYGEEYES NWFPALEEMV GKRYLNTEAS
HVSARPIPTC LRTSAIISEM NAGRGPIHMV TMEAFQDPHL EEVGWENFLG MTVGQAVLWA
ATDIDPKYIN PELTTSEPYV MGSHATACGA WCSGPEDLSP EEYFWGYNRM TSVEGLFGAG
DAVGGTPHAF SSGSFTEGRL AAKAACQYID DGKGEGIVVS DKQIADRKEE IYRPLETYRI
GRNEIVAGTV SPSYILPMPG LQRLQKIMDE YCGGVTVSYM TNDKLLNMGM QKMSIMEEDL
EKLGAEDIHQ LMRAWELKHR HRTSECVFQH TFFRKETRWP GYYYRGDAMK LDDDNWHVLT
VSHRDRETGE YTMAKAPCYH LVNDE
//
