ID J9ZAH6_LEPFM Unreviewed; 577 AA.
AC J9ZAH6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative adenylylsulfate reductase, subunit A {ECO:0000313|EMBL:AFS52727.1};
GN OrderedLocusNames=LFML04_0489 {ECO:0000313|EMBL:AFS52727.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS52727.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS52727.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS52727.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002919; AFS52727.1; -; Genomic_DNA.
DR RefSeq; WP_014960247.1; NC_018649.1.
DR AlphaFoldDB; J9ZAH6; -.
DR STRING; 1048260.LFML04_0489; -.
DR KEGG; lfi:LFML04_0489; -.
DR PATRIC; fig|1048260.3.peg.527; -.
DR HOGENOM; CLU_014312_8_3_0; -.
DR Proteomes; UP000006177; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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 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 PRINTS; PR00368; FADPNR.
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 10..380
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 443..559
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 577 AA; 63181 MW; 3F13FC1C148A72AD CRC64;
MAETIVIDTD IAIIGGGAAG CYAAMTARRK APDLDVLILE KAHIDRSGCL AGGMNAINAY
INPGESVDSF VEYVRFDAMG ILREDLVRTQ AALLNEVVRD LEQLGLPVVK DDSGRYAPRG
RWNIKIHGES LKPLLATAVR NLGARVLNRV VVTNLLVQDG SVAGCFGFGL RDGRFYVVRA
RKTIVATGGA SGLYRPNNEG DARHKMWYSP FNTGAGYAIG IRAGAEMTSF EHRFIALRTK
ETIAPTGTLA LGFGAPQVNA LGEEFMKKRW SHMGGEGAPT PIRLFAPLKE MAEGRGPCYM
DTRHLSAERV KALKEAYLDM YPNTVQYWAA NGIDPAREPI EICGTEPYIV GGHCQAGYWI
GVDRKTTLDN LFAAGDVAGG APYKFVSGCF AEGRIAAESA IREIRETPGA LPKMSPGVIE
REKMRVFSPL GAGGKLSPVA VEERLQKIMD EYAGGIRTQY AMNETSLKVA RKKLAEMLRD
LSSLAASDLH ELMNLHEVLD RIDVARVLVE HLMARKETRW PGFQTRLDFP ETREEWSLFV
NSASDPETGD IRIILRPLDS FSDSVTEPTE VVLGNPY
//
