COFG_SYNY3
ID COFG_SYNY3 Reviewed; 313 AA.
AC P73191;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase {ECO:0000255|HAMAP-Rule:MF_01611};
DE EC=4.3.1.32 {ECO:0000255|HAMAP-Rule:MF_01611};
DE AltName: Full=FO synthase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01611};
GN Name=cofG {ECO:0000255|HAMAP-Rule:MF_01611}; OrderedLocusNames=sll1285;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-
CC ribitylimino)-5,6-dihydrouracil. {ECO:0000255|HAMAP-Rule:MF_01611}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-
CC dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-
CC didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine +
CC NH4(+); Xref=Rhea:RHEA:55204, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:59904, ChEBI:CHEBI:85936; EC=4.3.1.32;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01611};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01611};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_01611};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01611}.
CC -!- SUBUNIT: Consists of two subunits, CofG and CofH. {ECO:0000255|HAMAP-
CC Rule:MF_01611}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofG family.
CC {ECO:0000255|HAMAP-Rule:MF_01611}.
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; BA000022; BAA17217.1; -; Genomic_DNA.
DR PIR; S75303; S75303.
DR AlphaFoldDB; P73191; -.
DR SMR; P73191; -.
DR STRING; 1148.1652294; -.
DR PaxDb; P73191; -.
DR EnsemblBacteria; BAA17217; BAA17217; BAA17217.
DR KEGG; syn:sll1285; -.
DR eggNOG; COG1060; Bacteria.
DR InParanoid; P73191; -.
DR OMA; TTACRYT; -.
DR PhylomeDB; P73191; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IBA:GO_Central.
DR GO; GO:0016841; F:ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01611; FO_synth_sub1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR019939; CofG_family.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03550; F420_cofG; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..313
FT /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT /id="PRO_0000147759"
FT DOMAIN 4..235
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01611"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01611"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01611"
SQ SEQUENCE 313 AA; 35288 MW; 3DF30B0649C0EA16 CRC64;
MLSITYSPAY TLVPTYECFN RCSYCNFRQE PRKDQWLTES VAKQRLESLA GRGIREILIL
AGEVHPQSSR RKAWFELIYN LGKIALDLGF YPHTNAGPLS RSEIARLKEV NFSLGLMLEQ
VSPRLLTTVH RQAPSKEPQL RLEQLRLAGE LGIPFTTGLL LGIGETDQEV EESLMAIANV
QQEYGHIQEV ILQPHSPGQK QTDNISAYSP QKLVQVITLA RAILPAEITL QIPPNLVPNF
SDLLACLAAG VRDLGGIVPI DEVNPDYHHQ SVNQLSQLLE ENGYLLQPRF PVYPTYFSWL
NCDLQQRLSV FIN
