ID F7NHI3_9FIRM Unreviewed; 453 AA.
AC F7NHI3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:EGO64530.1};
GN ORFNames=ALO_07653 {ECO:0000313|EMBL:EGO64530.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO64530.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO64530.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO64530.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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:EGO64530.1}.
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DR EMBL; AFGF01000054; EGO64530.1; -; Genomic_DNA.
DR RefSeq; WP_004094340.1; NZ_AFGF01000054.1.
DR AlphaFoldDB; F7NHI3; -.
DR STRING; 1009370.ALO_07653; -.
DR eggNOG; COG0641; Bacteria.
DR OrthoDB; 9808591at2; -.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21124; SPASM_CteB-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR024025; SCIFF_rSAM_maturase.
DR InterPro; IPR047602; SPASM_CteB-like.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR03974; rSAM_six_Cys; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF8; RADICAL SAM PROTEIN-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDG01216; thioether_bond_formation_requi; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 89..321
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 453 AA; 50643 MW; 50743B0BA224752F CRC64;
MKKSIHTFTQ GDLHILLDVN SGAVHLIDGM TQDILQVFEG GNDQAVLNAL SGHYDRGDVT
EALEELHQLM DQGLLFAPEL SLPDVFRQKP VVKSLCLHVA HDCNLRCGYC FAGTGAFGHQ
RGLMDATVGK KAIDFLIEHG GDRRYAEIDF FGGEPLLNME TVRAVTDYSR QRGQETGKIF
RLTLTTNAVL LDDATIQYLN DNDISVVLSL DGRRQTHDRM RPRTGGAGSF DECVQNITKL
VQSRNDQNYY VRGTFTAWNL DFAADVLAMA DLGFTRLSVE PVVAKGAAYG IESRHLPELF
RQYDLLTEEY LRRKEQGVGF DFFHFNVDIN NGPCVAKRLS GCGAGHEYFA VTPDGDLYPC
HQFVGRDGFC VGSVFDGIQR PEIGQRFRDA DVLTKEACRS CWAKFYCSGG CHANADLFHG
RLDQPYEIGC ELQRKRLECA IYIQAKLALT REK
//
