ID B1MLI0_MYCA9 Unreviewed; 881 AA.
AC B1MLI0;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=MAB_1319 {ECO:0000313|EMBL:CAM61407.1};
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS abscessus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM61407.1, ECO:0000313|Proteomes:UP000007137};
RN [1] {ECO:0000313|EMBL:CAM61407.1, ECO:0000313|Proteomes:UP000007137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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}.
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DR EMBL; CU458896; CAM61407.1; -; Genomic_DNA.
DR AlphaFoldDB; B1MLI0; -.
DR KEGG; mab:MAB_1319; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000007137; 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; 1.
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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 106..358
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 567..808
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 881 AA; 95637 MW; 5D94ECECD9C90D5D CRC64;
MMNPRVVGFS VRADDLRVTD GCTNVPDDVT PLPNPAFPSR KAASSTALRR VLRRARDGVT
LNVDEAALAL TARGDDLADL MASAARVRDA GLESGGRLGA EGRLPISYSR KVFIPVTHLC
RDKCHYCTFV TVPGKLRAQG QGMYMEPDEI LDVARRGAEL GCKEALFTLG DRPEERWPEA
KQWLDERGYD TTLDYVRAMA IRVLEETGLL PHLNPGVMSW AELARLKPVA PSMGMMLETT
SRRLFEDRGE AHYGSPDKDP AVRLRTLTDA GRLSIPFTTG LLVGIGENLT ERAETIHAIR
KVHKEFGHVQ EVIVQNFRAK SDTAMKSAPD ADIDDFLATI AVTRLVLGPK MRVQAPPNLV
SRSECLALIG AGVDDWGGVS PLTPDHVNPE RPWPALDDLA SVTAEAGYDL VQRLTAQPQY
VQAGAAWIDP RVRGHVEALA NPETGYALDI SPTGLPWQEP DETWESTGRV DLHAAIDSEG
RNTDTRSDLA SAFGDWESIR EHVRELNARA PEKVGADVLA ALRSAERDPA GCTDDEYLAL
ATAEGPAMDA LAALADSIRA DVVGDDVTYV VNRNINFTNI CYTGCRFCAF AQRKGDADAF
SLSAEEVGDR AWEAYVAGAT EVCMQGGIDP ELPVTGYADL VRAVKKRVPS MHVHAFSPME
IVNGASKGGQ SVRDWLTELR AAGLDTIPGT AAEILDDEIR WVLTKGKLPA SEWIDVISTA
HEVGLRSSST MMYGHVDTPK HWVAHLRVLA GIQDRTGGFT EFVPLPFVHQ SAPLYLAGAA
RPGPTNRDNR AVHALARIML HGRIDNIQTS WVKLGIEGTR VMLQSGANDL GGTLMEETIS
RMAGSEHGSA KTIAELEEIA DGIGRPAVER TTTYARRPSA A
//
