FBIC_MYCPA
ID FBIC_MYCPA Reviewed; 867 AA.
AC Q73WP9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=FO synthase;
DE Includes:
DE RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase;
DE EC=4.3.1.32;
DE Includes:
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase;
DE EC=2.5.1.147;
GN Name=fbiC; OrderedLocusNames=MAP_2611c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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.
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 -!- 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. The clusters are coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. CofG family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the radical SAM
CC superfamily. CofH family. {ECO:0000305}.
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DR EMBL; AE016958; AAS04928.1; -; Genomic_DNA.
DR AlphaFoldDB; Q73WP9; -.
DR SMR; Q73WP9; -.
DR STRING; 262316.MAP_2611c; -.
DR EnsemblBacteria; AAS04928; AAS04928; MAP_2611c.
DR KEGG; mpa:MAP_2611c; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_010522_1_0_11; -.
DR OMA; HWVGHLN; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000580; 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; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 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/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 2.
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; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 2.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03550; F420_cofG; 1.
DR TIGRFAMs; TIGR03551; F420_cofH; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..867
FT /note="FO synthase"
FT /id="PRO_0000147771"
FT DOMAIN 92..344
FT /note="Radical SAM core 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 555..796
FT /note="Radical SAM core 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..425
FT /note="CofG-like"
FT REGION 532..865
FT /note="CofH-like"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 573
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 867 AA; 93483 MW; D431F04B2BC67636 CRC64;
MLLTPGEEPT ALPDPVVPAR ASSRATPKAT ASALRRVLRR ARDGVALNID EAAVAMTARG
DDLADLCASA ARVRDAGLQS AGRRGPGGGL PITYSRKVFI PVTHLCRDNC HYCTFVTVPG
KLRARGAGLY LEPDEILDIA RRGGELGCKE ALFTLGDRPE DRWPEAREWL EARGYDSTLS
YVRAMAIRVL EETGLLPHLN PGVMSWSEMA RLKPVAPSMG MMLETTSRRL FETKGLAHYG
SPDKDPAVRL RTLTDAGRLS IPFTTGLLVG IGETPAERAD TLHAIRKSHK EFGHVQEVIV
QNFRAKEHTA MAAVPDAGIE DYLATVAVAR LVLGPGMRIQ APPNLVSRDE CRALIAAGVD
DWGGVSPLTP DHVNPERPWP ALDELAAVTA ESGYELVQRL TAQPKYVQAG AAWIDPRVSG
HVRALADPVT GLARDVNPVG LPWQEPDDVG SSGRVDLNAA IDTQGRNSET CSDIDSAFGD
WESIRAHVHE LAAQGARAPE RLDSDVLAAL RSAERDPAGC TDSEYLSLAT ADGPALEAVA
ALADSLRRDT VGDDVTFVVN RNINFTNICY TGCRFCAFAQ RKGDADAYSL STEEVADRAW
EAHVAGATEV CMQGGIDPEL PVTGYADLVR AVKARVPSMH VHAFSPMEIA NGVTKSGLSI
REWLISLREA GLDTIPGTAA EILDDEVRWV LTKGKLPTSL WIEIVTTAHE VGLRSSSTMM
YGHVDNPRHW VGHLNVLRDI QDRTGGFTEF VPLPFVHQSS PLYLAGAARP GPTHRDNRAV
HALARIMLHG RISQIQTSWV KLGVQRTQVM LNGGANDLGG TLMEETISRM AGSEHGSAKT
VAELTAIAEG IGRPARQRTT DYTPLAA
