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Database: UniProt
Entry: F0H2T2_9FIRM
LinkDB: F0H2T2_9FIRM
Original site: F0H2T2_9FIRM 
ID   F0H2T2_9FIRM            Unreviewed;       729 AA.
AC   F0H2T2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:EGC83256.1};
GN   ORFNames=HMPREF9246_0381 {ECO:0000313|EMBL:EGC83256.1};
OS   Anaerococcus hydrogenalis ACS-025-V-Sch4.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC83256.1, ECO:0000313|Proteomes:UP000005277};
RN   [1] {ECO:0000313|EMBL:EGC83256.1, ECO:0000313|Proteomes:UP000005277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC83256.1,
RC   ECO:0000313|Proteomes:UP000005277};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGC83256.1}.
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DR   EMBL; AEXN01000039; EGC83256.1; -; Genomic_DNA.
DR   RefSeq; WP_004818424.1; NZ_AEXN01000039.1.
DR   AlphaFoldDB; F0H2T2; -.
DR   OrthoDB; 1737006at2; -.
DR   Proteomes; UP000005277; 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   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR026401; CXXX_matur.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR026412; rSAM_Cxxx_rpt.
DR   InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR   NCBIfam; TIGR04119; CXXX_matur; 1.
DR   NCBIfam; TIGR04115; rSAM_Cxxx_rpt; 1.
DR   NCBIfam; TIGR04085; rSAM_more_4Fe4S; 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   SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR   SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          28..179
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|Pfam:PF04055"
SQ   SEQUENCE   729 AA;  85262 MW;  E27F6AEA302CE028 CRC64;
     MIKNNITYKL GKEINIWKDG LAQTLTFIVT EDCNLRCNYC YITHKSSNKK MSFEVAKKFI
     DYVLTEEMIR PKGVILDFIG GEPLLEIKLI DQICDYFKLK TYLLNDEWFW DYRINITTNG
     INYASKEVQD FIKKNQGKLE IAITLDGTKE KHDMHRIFPN GKGSYDEIIR NIELYKNQFQ
     ASTKVTFSSK DLKYLKDSII HLWELGISDV AANVVFEDVW QDGDEKTFED QLIELADYIL
     ENRLFDKYSC TLFDESIGSP NSREMLETAS CGAGKMIAVG PDGSLYPCMR YKDYSLNNKK
     EIAIGDVENG IDFDKIRPYY LINTQLQSDE ECLNCRIASG CTSCFGHNYD SADSNTNFQK
     AKYICKMHKA RVRANNYYFA ELYNRYGIER EINNEERDKL YFLLSNSAVR TCTSSEDRSD
     LSIMSDETIK QGLEYAKNNF LRPVFIHSNY GLNLNFKEID LKGHNIFHYC SIRNQDSIRK
     ITNNYILTIE YPNDEEFVKN MKLEENIILN ISSDYLSDIE NFVTKLFNKT NRINLNILDI
     DKQFNYTLYE NQLKNISDYI YYEYLNKGII KELNVITDEM FMEEKELCDS GLNSYTLASN
     EKFYVCPEFY FNFPLDYIGS LKDGIKEKYN RHLYSEKYSP LCNKCSICHC NSCSFENYIN
     TNEVNIPAKN SCVKSSIEYR VSYELQKKLS KLMEFDIHIK PLNYLDPFVD VLEKNPVNGI
     LNKKYLEDN
//
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