ID L8X9K4_THACA Unreviewed; 1404 AA.
AC L8X9K4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664};
DE EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664};
GN ORFNames=AG1IA_00224 {ECO:0000313|EMBL:ELU45763.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU45763.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU45763.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001697};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2. {ECO:0000256|ARBA:ARBA00004917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424}.
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:ELU45763.1}.
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; AFRT01000039; ELU45763.1; -; Genomic_DNA.
DR STRING; 983506.L8X9K4; -.
DR HOGENOM; CLU_254119_0_0_1; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01846; fatty_acyltransferase_like; 1.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1.
DR Gene3D; 3.10.20.870; PFU (PLAA family ubiquitin binding), C-terminal domain; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR InterPro; IPR015155; PFU.
DR InterPro; IPR038122; PFU_sf.
DR InterPro; IPR013535; PUL_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR NCBIfam; TIGR00114; lumazine-synth; 1.
DR PANTHER; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR19849:SF0; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR Pfam; PF00885; DMRL_synthase; 2.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR Pfam; PF09070; PFU; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51394; PFU; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 449..480
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 488..519
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 527..562
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 570..602
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 711..809
FT /note="PFU"
FT /evidence="ECO:0000259|PROSITE:PS51394"
FT DOMAIN 865..1157
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
FT REGION 301..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1404 AA; 152325 MW; C5147EF7AB2AF709 CRC64;
MFSSGLMCTN FAVFHNYVPG FSLSRRNYGF LQINISIDLG IDKATTGYNV SAGINSPTPG
WTSSNGPNWV QYLGGTYNVT DTKVRMSGIS AIKSYGFGWV LLLQVYNLAY GGATTDSKLV
TPYLPTVQSF VDQVTLFSNH FSPVPAEAPW TSDNSLFGIW IGINDIASLF DSIELKAAGF
HQTLLDRYFS QVDELYRRGA RSFLFLNVPP LERAPLFIEQ GATTVKAVMA STDDFNKQLA
QRVKQFQKTY KGLGQVTLYD AHKAFNVQLL VSPRCLSFVN WLTRVSQKLV ELASSYVRSP
RRSNLPPQKA NLISPDSGLD QTTSLKDNPQ PWWVLLAGLY NMGHLYKLSA VLSAHSSDVR
DLIAPTNDLI LSVSRDSLAI AWRRDGPNGF TPTTYSAGSR FVNSVTYIPP QKNGGPGSQG
YIVTGGQDTV INVFDLSHPD GAKEPTFTLL GHRENVCALD STPSGTIVSG SWDSTARVWK
NFQQVHELRG HSHSVWAVLA VDEDQTLTGS ADKTIALWQG SKLAHRYTGH TDAVRGLSIL
PEGIDIGFAS CSNDGTVKLW TLGGDVLHQF DGHTSFVYSL AAIAETGSLI SSGEDRTARI
WEDGELVQTL THPAISVWTV DAMPNGDIVT GCSDGVVRVF SRNESRWANA ETIQVSSFGT
TIVASQAIPS ESVGDVKKTD LPGPEALERS GNKDGQVIMV RTASGSVEAH EWSAGQRKWV
KIGDVVDAVG QNRKQLYNGK EYDYVFKVDI KDGAPPLSLP YNATVCADNP YSAAQKFLAE
NELSMEYIDQ VVGFIEKNTG GFKVEQQSQQ FVDPYTGASR YQANPTSAPS NNITTYSDPF
TGGSRYAPAS THAAATPPPP KPVNSILPVR TALGFKQANI PAMENKFKQL NEGLSGDPNT
SSLALTPLEF KLFNRSFALM NAKAHSPPKV PVETSAELSQ KDIDIIADVL ARWPSLQRFP
GRYLRCGFML LIAYSPNTFE APQTSQKLID ALFEASEWKS EPWPSPLPKH RETNVLLTLR
ALSNLFQVGP HKVVGTGPWV PGLFTTLAAG PYSVLTKTQK VALATIAFKE DNETGYRALV
ALGNIVSESF NQGSLSDVAA AAYRPLLTNV ATAFPEERTA CIQHCKLCYA PVNSSPASAL
SASRLAVKHS KQLIKPRGMQ PKNSDNRVLR VFSHHPAFTF IHPRLYKTMS DPTIKGLVPS
QVEYDGSNLR VAIVHARWNK TVIDALVAGA VEKLKERGVK ESNIVIESVP GSFELPLACS
KVISASQTQA SSTATDLLGG AASLLSLDPH APQRIPSPAP GTVTVNMPSK AFDAVIAIGV
LIKGSTMHFE YICDSVSHAL MRLQMDTGVP VIFGVLTALT DDQALERAGL GRGPNGKGHN
HGEDWGLAAV EMGSHVQKWA AGKF
//
