ID B8HSF7_CYAP4 Unreviewed; 554 AA.
AC B8HSF7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ACL44263.1};
GN OrderedLocusNames=Cyan7425_1896 {ECO:0000313|EMBL:ACL44263.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL44263.1};
RN [1] {ECO:0000313|EMBL:ACL44263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL44263.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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; CP001344; ACL44263.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HSF7; -.
DR STRING; 395961.Cyan7425_1896; -.
DR KEGG; cyn:Cyan7425_1896; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_021572_5_0_3; -.
DR OrthoDB; 9801424at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR025274; DUF4070.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034530; HpnP-like.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR PANTHER; PTHR43409:SF9; BLR2995 PROTEIN; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF13282; DUF4070; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00303; hopanoid_C2-methyltransferase; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 195..428
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 63485 MW; 71A953C1CC3E1BB1 CRC64;
MVADPKAFEQ TVPEMTGEHT PYSPRNHRRI LCVFPRYSRS FGTFHHAYSL MGRDVRAFMP
PQGILLVAAY MPASWEVRLV DENVTPATEA DYRWADVVIT SGMHIQRPQI NQINEIAHRL
GKLTVVGGPS VSGCPEYYPD FDILHLGELG DATDRMIEYF DLHGSTRPPA QLRFETLERL
PLSQFPVPAY NLVNVRNYFL GSVQFSSGCP FRCEFCDIPE LYGRNPRLKT PEQILQELDT
MLASGNPGAV YFVDDNFIGN RRAVTELLPH LIDWQKRNGY PIQFACEATL NIAQSPKLLE
MMREAYFCTV FCGIETPEPD ALHAISKDQN LSMPILEAIK TLNRYGMEVV SGIIIGLDTD
TPQTGDRILD FIRASQIPTL TINLLHALPR TPLWRRLEAE GRLNYDENRE SNVEFLMPYE
EVVEMWRRTI TTAYEPEFLY QRFDYQCQNT FPNRIKPPNS PARVSRENVN KGLRALRNII
WQVGVLSDYR RTFWKYNWPR LKAGKIESVI STSLVSHHLI KFAQECGRGD EAAAFYAQRV
EQKPEGLQLV SPRS
//
