ID E2SFM8_9ACTN Unreviewed; 848 AA.
AC E2SFM8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=FO synthase {ECO:0000256|ARBA:ARBA00022220};
DE EC=2.5.1.147 {ECO:0000256|ARBA:ARBA00012289};
DE EC=4.3.1.32 {ECO:0000256|ARBA:ARBA00012126};
GN Name=cofH {ECO:0000313|EMBL:EFQ81995.1};
GN ORFNames=HMPREF0063_12837 {ECO:0000313|EMBL:EFQ81995.1};
OS Aeromicrobium marinum DSM 15272.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=585531 {ECO:0000313|EMBL:EFQ81995.1, ECO:0000313|Proteomes:UP000003111};
RN [1] {ECO:0000313|EMBL:EFQ81995.1, ECO:0000313|Proteomes:UP000003111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15272 {ECO:0000313|EMBL:EFQ81995.1,
RC ECO:0000313|Proteomes:UP000003111};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin (FO) from 5-amino-6-(D-ribitylamino)uracil
CC and L-tyrosine. {ECO:0000256|ARBA:ARBA00003692}.
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:0000256|ARBA:ARBA00000328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-
CC methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-
CC hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-
CC methionine; Xref=Rhea:RHEA:55200, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15934, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:59789, ChEBI:CHEBI:77846,
CC ChEBI:CHEBI:85936; EC=2.5.1.147;
CC Evidence={ECO:0000256|ARBA:ARBA00000403};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004712}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the radical SAM
CC superfamily. CofH family. {ECO:0000256|ARBA:ARBA00010051}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. CofG family. {ECO:0000256|ARBA:ARBA00010826}.
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:EFQ81995.1}.
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DR EMBL; ACLF03000013; EFQ81995.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SFM8; -.
DR STRING; 585531.HMPREF0063_12837; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_010522_1_0_11; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000003111; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0141093; F:5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR HAMAP; MF_01611; FO_synth_sub1; 1.
DR HAMAP; MF_01612; FO_synth_sub2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR019939; CofG_family.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR019940; CofH_family.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00423; CofH family radical SAM protein; 1.
DR NCBIfam; TIGR03550; F420_cofG; 1.
DR NCBIfam; TIGR03551; F420_cofH; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 2.
DR SFLD; SFLDF00293; ((2_3_4_5-tetrahydroxypentyl)a; 1.
DR SFLD; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SFLD; SFLDG01388; 7_8-didemethyl-8-hydroxy-5-dea; 2.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 2.
DR PROSITE; PS51918; RADICAL_SAM; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000003111};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:EFQ81995.1}.
FT DOMAIN 77..329
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 532..768
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 91053 MW; 86CB73958A8C1727 CRC64;
MVAVHLPFPG VPPVGSSRPT DGEVRRAVVR AEAGKSLDTS EVAALLASTG EHLDRLMAVA
ARVRDAGLAA VGRSGVVTFS PKVFVPVTRL CRDRCHYCTF VATPGQLERD GQGLFLSVDE
VLEICRAGAG LGCTEALFTL GDRPEDRWPE AKRWLAEAGY DSTLEYVRAL AVRVLEETGL
LPHLNPGVMS WAEMNRLKPV APSMGMMLET TSERLFTEKG QPHHGSPDKD PAVRLRVLED
AGRLGIPFTT GILVGIGETW VERAESLFAI RRVHREHGSI QEVIVQNFRA KDATAMRSTD
DLGVEEYLAA VATARVVLGP GVRVQAPPNL VDLAECGQLL AAGVDDFGGI SPVTPDHVNP
ERPWPQIDAL RGVCEAGGFD LRPRLTTHPE LLDAPWVDPR LRPHVDALRG PDGLLADGVR
PVGLPWQEPD GGLVTSGRSD LHASIDTTGR RADRRGDFDE VYGDWDTIGA RVPAAPERLA
GDVAAALRAA ERDPAGLTEA QALALMTADG PGLEAVCALA DDLRRDTVGD TVTYVVNRNI
NFTNICYTGC RFCAFAQRAT DADAYSLSTD EIADRVREAV AVGATEVCVQ GGIDPSLPGT
VYADIARTIK AAGPDLHLHA YSPMEVMNGV ARTGLSITEF LHSLAEAGVD SLPGTAAEIL
DDDVRWVLTK GKLPASQWIE VVRTAHTIGL PTTATMMYGH VDHPGHWVTH LKVIADLQRD
TGGFTEFVPL PFVHQSSPIY LAGVARPGPT VRDNRAVHAM ARIMLHGLVD NIQCSWVKLG
PDQCTQVLNG GVNDLGGTLM EETISRMAGS TNGSRKERED LEAMAHLAGR PARQRTTTYG
RLPAASPA
//
