ID A0A101W853_9FLAO Unreviewed; 647 AA.
AC A0A101W853;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=YgiQ family radical SAM protein {ECO:0000313|EMBL:KUO68147.1};
GN ORFNames=APF83_00440 {ECO:0000313|EMBL:KUO68147.1};
OS Lutibacter sp. BRH_c52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO68147.1, ECO:0000313|Proteomes:UP000054346};
RN [1] {ECO:0000313|EMBL:KUO68147.1, ECO:0000313|Proteomes:UP000054346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO68147.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01251};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|HAMAP-Rule:MF_01251};
CC -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000256|HAMAP-
CC Rule:MF_01251}.
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:KUO68147.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOEY01000027; KUO68147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101W853; -.
DR Proteomes; UP000054346; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR HAMAP; MF_01251; UPF0313; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR022946; UPF0313.
DR InterPro; IPR024560; UPF0313_C.
DR InterPro; IPR013704; UPF0313_N.
DR NCBIfam; TIGR03904; SAM_YgiQ; 1.
DR PANTHER; PTHR32331; UPF0313 PROTEIN YGIQ; 1.
DR PANTHER; PTHR32331:SF0; UPF0313 PROTEIN YGIQ; 1.
DR Pfam; PF11842; DUF3362; 1.
DR Pfam; PF08497; Radical_SAM_N; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01069; UPF0313; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01251};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01251};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01251};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01251};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01251}.
FT DOMAIN 303..583
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 317
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
FT BINDING 321
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
FT BINDING 324
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
SQ SEQUENCE 647 AA; 73657 MW; 9B8F77B121145E16 CRC64;
MMNKLSDWLP TTNKEVKLRG WDELDVILFT GDAYVDHPAF GAAVIGRLLE SYGLRVAIVP
QPSVHDNLQD FTKLGTPKLF FAVTGGCMDP MVSNYTASKR KRDNDAYTPN GDKGFRPDYA
TTVYSTILKE KFPEVPVLIG GIEASLRRVT HYDYWSDTLK PTILIDSKAD LLVYGMGEQP
LQEIVNLLKK GVPFSSIRTV KQTAFLVDKN DEIPKNKNWE DVSINSHEVC LKDKKSYAAN
FKVIEQESNK LHANRVLQGV NNSTLVINPP YETMTEAEID ASFDLPYTRL PHPKYNLRGP
IPAFEMIKFS INIHRGCFGG CSFCTISAHQ GKFIASRSQE SILKEVDKVA NMPDFKGYLS
DIGGPSANMY KMKGKVQEIC DRCVSPSCIS PVICHNLDTS HKPLTELYKA VDRHPKVKKS
FIGSGIRHDL LVPEFNKLAD PKELDAYTEE VMTNHISGRL KVAPEHTSDN VLKLMRKPSF
SYFHKFKERF DAINIRKKLN LQLIPYFISS HPASELEDMA NLAAETKDLG FQLEQVQGFT
PTPMTVATVI YYSGYHPYTL KPTKTPKTKQ EREDQHRFFF WYKKENQQWI RNTLTKVGRT
DLLQKLLPEN NNWRKNKNAA AKDTFNDTIP FVKKNKGKFF KKNKAKN
//
