ID A0A137SV78_9FIRM Unreviewed; 431 AA.
AC A0A137SV78;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:KXO16365.1};
GN ORFNames=HMPREF3189_00768 {ECO:0000313|EMBL:KXO16365.1};
OS Clostridiales bacterium KA00134.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO16365.1, ECO:0000313|Proteomes:UP000070500};
RN [1] {ECO:0000313|EMBL:KXO16365.1, ECO:0000313|Proteomes:UP000070500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00134 {ECO:0000313|EMBL:KXO16365.1,
RC ECO:0000313|Proteomes:UP000070500};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005155}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. NifB family.
CC {ECO:0000256|ARBA:ARBA00006804}.
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:KXO16365.1}.
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DR EMBL; LTAF01000021; KXO16365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137SV78; -.
DR STRING; 1588750.HMPREF3189_00768; -.
DR OrthoDB; 9808591at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000070500; 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 GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR PANTHER; PTHR43787:SF3; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB; 1.
DR PANTHER; PTHR43787; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01386; main_SPASM_domain-containing; 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 Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000070500};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 82..316
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 431 AA; 49388 MW; 75E0C9D922E5C518 CRC64;
MKKSKYNFKV DLEGRSEYIL YNSKTNALAV LEGDEISAYE EEKFEGLGTK MKNNFLQGGF
LVEDDIDELE EIRFRLNRSR YSTSSLSLTI ALTADCNFRC AYCYEKENLK DSYMTKKHRE
NIVRFVEDAA KNGLGSLNIT WYGGEPLLAF SDLKYLAENF LRLKEQYKFN YFSFMVSNGF
LLNRKIVEEL NRLQVSGYQI TIDGDEKSHN KKRFLKGGGA TYRTILDNLK NSIDILPNIS
LRINVDKQNI DKINGLISEL ESINKDDKIS TYLGKVENYK SLYADSLCLS DVEFSKKEFE
FFKGTYPSAI LEKYPNLRGN FCGADGLSSY VMASDGKVFK CWSDIGYEKT AIGHLTEDGI
SLNNRSYYLD LMNFDPTSDK ECSACAYLPI CMGGCPYDRI NKKQKTCLKN NYYFDGYIKE
ITSLLLGNPF N
//
