ID E4U2M7_SULKY Unreviewed; 579 AA.
AC E4U2M7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ADR33612.1};
GN OrderedLocusNames=Sulku_0948 {ECO:0000313|EMBL:ADR33612.1};
OS Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 /
OS YK-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfuricurvum.
OX NCBI_TaxID=709032 {ECO:0000313|EMBL:ADR33612.1, ECO:0000313|Proteomes:UP000008721};
RN [1] {ECO:0000313|EMBL:ADR33612.1, ECO:0000313|Proteomes:UP000008721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1
RC {ECO:0000313|Proteomes:UP000008721};
RX PubMed=22675602; DOI=10.4056/sigs.2456004;
RA Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of the sulfur compounds oxidizing
RT chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).";
RL Stand. Genomic Sci. 6:94-103(2012).
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 ---------------------------------------------------------------------------
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; CP002355; ADR33612.1; -; Genomic_DNA.
DR AlphaFoldDB; E4U2M7; -.
DR STRING; 709032.Sulku_0948; -.
DR KEGG; sku:Sulku_0948; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_018288_2_0_7; -.
DR OrthoDB; 9803479at2; -.
DR Proteomes; UP000008721; Chromosome.
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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008721};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01251}.
FT DOMAIN 295..569
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 309
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 313
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 316
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 579 AA; 66243 MW; 20D91CFDB752A1F3 CRC64;
MKTITPEHLR YLPTTRAEMD ERGWDRCDVI LISGDAYIDS PFIGVAVVGR ILEREGYRVG
IIGQPDINTD DVMRLGEPKL FWGVSGGSVD SMVSNYTATK KFRNSDDYTP GGVNNARPDR
ATLVYTNLIR KHFKNTVPIV LGGIEASLRR VTHYDYWTNK LRKPILFDSK ADYLIYGMGE
GAIIALPKAL ERGESPNDIR GVCYIAKEPR EEYLKLPSHQ ECLDNKERYI DLFDTFYNNN
DPISAKGLCQ EVDGRYAIQN PPADYLDESE MDAVSSLPFT RELHPYHRPK GSVKCLETIK
FSIMTHQGCW GECNFCAIGV HQGRTIRTRS EESILKEATQ FTEYKDFKGI ISDVGGPTAN
MYGYECNKKL KHGTCDHQRC VDDTHLCKSM KVDHTRVINL LRRLREVRGV KKAFVASGVR
YDLINEDKRQ GYEYLKEMVR HHISGQMKVA PEHTSEHVLH LMNKPGKQTL VDFKKLYDKL
NREEGKKQFL TYYLIAAHPG CTEKDMHDLK RFTSEELKMN PEQAQVFTPT PGTYSAVMYY
TEMDPATRKK IFVEKDTARK EKQKQIVVAK ESFKSGFAS
//
