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6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) (Riboflavin biosynthesis protein RibBA) [Includes: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)]

 A0A1C4SBV0_9ACTN        Unreviewed;       613 AA.
A0A1C4SBV0;
02-NOV-2016, integrated into UniProtKB/TrEMBL.
02-NOV-2016, sequence version 1.
05-DEC-2018, entry version 23.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|HAMAP-Rule:MF_01283};
Includes:
RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283};
Includes:
RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01283};
Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_01283};
EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_01283};
Includes:
RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_01283};
EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_01283};
AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_01283};
Includes:
RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178};
Short=DMRL synthase {ECO:0000256|HAMAP-Rule:MF_00178};
Short=LS {ECO:0000256|HAMAP-Rule:MF_00178};
Short=Lumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178};
EC=2.5.1.78 {ECO:0000256|HAMAP-Rule:MF_00178};
Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283};
Synonyms=ribH {ECO:0000256|HAMAP-Rule:MF_00178};
ORFNames=GA0115236_158411 {ECO:0000313|EMBL:SCE44731.1};
Streptomyces sp. IgraMP-1.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1839767 {ECO:0000313|EMBL:SCE44731.1, ECO:0000313|Proteomes:UP000199536};
[1] {ECO:0000313|EMBL:SCE44731.1, ECO:0000313|Proteomes:UP000199536}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IgraMP-1 {ECO:0000313|EMBL:SCE44731.1,
ECO:0000313|Proteomes:UP000199536};
Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
formate and 3,4-dihydroxy-2-butanone 4-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
-!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_01283}.
-!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-
ribityllumazine by condensation of 5-amino-6-(D-
ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate.
This is the penultimate step in the biosynthesis of riboflavin.
{ECO:0000256|HAMAP-Rule:MF_00178}.
-!- CATALYTIC ACTIVITY:
Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine +
H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830;
EC=2.5.1.78; Evidence={ECO:0000256|HAMAP-Rule:MF_00178};
-!- CATALYTIC ACTIVITY:
Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl
phosphate + formate + H(+); Xref=Rhea:RHEA:18457,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58121,
ChEBI:CHEBI:58830; EC=4.1.99.12; Evidence={ECO:0000256|HAMAP-
Rule:MF_01283};
-!- CATALYTIC ACTIVITY:
Reaction=GTP + 3 H2O = 2,5-diamino-6-hydroxy-4-(5-
phosphoribosylamino)-pyrimidine + diphosphate + formate + 2
H(+); Xref=Rhea:RHEA:23704, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:33019,
ChEBI:CHEBI:37565, ChEBI:CHEBI:58614; EC=3.5.4.25;
Evidence={ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711742};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01283};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_01283};
Note=Binds 2 divalent metal cations per subunit. Magnesium or
manganese. {ECO:0000256|HAMAP-Rule:MF_01283};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_01283};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01283};
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
1/1. {ECO:0000256|HAMAP-Rule:MF_01283}.
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|HAMAP-
Rule:MF_01283, ECO:0000256|SAAS:SAAS00711724}.
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis;
riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
ribitylamino)uracil: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00178}.
-!- SIMILARITY: Belongs to the DMRL synthase family.
{ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS00579181}.
-!- SIMILARITY: In the C-terminal section; belongs to the GTP
cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00789992}.
-!- SIMILARITY: In the N-terminal section; belongs to the DHBP
synthase family. {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00534513}.
-----------------------------------------------------------------------
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EMBL; FMCM01000526; SCE44731.1; -; Genomic_DNA.
UniPathway; UPA00275; UER00399.
UniPathway; UPA00275; UER00400.
UniPathway; UPA00275; UER00404.
Proteomes; UP000199536; Unassembled WGS sequence.
GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00641; GTP_cyclohydro2; 1.
CDD; cd09209; Lumazine_synthase-I; 1.
Gene3D; 3.40.50.10990; -; 1.
Gene3D; 3.40.50.960; -; 1.
HAMAP; MF_00178; Lumazine_synth; 1.
HAMAP; MF_00179; RibA; 1.
HAMAP; MF_00180; RibB; 1.
HAMAP; MF_01283; RibBA; 1.
InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
InterPro; IPR000422; DHBP_synthase_RibB.
InterPro; IPR032677; GTP_cyclohydro_II.
InterPro; IPR034964; LS.
InterPro; IPR002180; LS/RS.
InterPro; IPR036467; LS/RS_sf.
InterPro; IPR000926; RibA.
InterPro; IPR036144; RibA-like_sf.
InterPro; IPR016299; Riboflavin_synth_RibBA.
Pfam; PF00926; DHBP_synthase; 1.
Pfam; PF00885; DMRL_synthase; 1.
Pfam; PF00925; GTP_cyclohydro2; 1.
SUPFAM; SSF142695; SSF142695; 1.
SUPFAM; SSF52121; SSF52121; 1.
SUPFAM; SSF55821; SSF55821; 1.
TIGRFAMs; TIGR00114; lumazine-synth; 1.
TIGRFAMs; TIGR00505; ribA; 1.
TIGRFAMs; TIGR00506; ribB; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000199536};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711691};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS01033620};
Lyase {ECO:0000256|HAMAP-Rule:MF_01283};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01283};
Manganese {ECO:0000256|HAMAP-Rule:MF_01283};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00037896};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711691};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00178,
ECO:0000256|SAAS:SAAS00106368};
Transferase {ECO:0000256|HAMAP-Rule:MF_00178,
ECO:0000256|SAAS:SAAS00470627};
Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}.
DOMAIN 226 391 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
NP_BIND 270 274 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
NP_BIND 314 316 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 1 219 DHBP synthase. {ECO:0000256|HAMAP-
Rule:MF_01283}.
REGION 43 44 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 158 162 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 220 613 GTP cyclohydrolase II.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 510 512 5-amino-6-(D-ribitylamino)uracil binding.
{ECO:0000256|HAMAP-Rule:MF_00178}.
REGION 533 535 5-amino-6-(D-ribitylamino)uracil binding.
{ECO:0000256|HAMAP-Rule:MF_00178}.
REGION 538 539 1-deoxy-L-glycero-tetrulose 4-phosphate
binding. {ECO:0000256|HAMAP-
Rule:MF_00178}.
ACT_SITE 348 348 Proton acceptor; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
ACT_SITE 350 350 Nucleophile; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
ACT_SITE 541 541 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00178}.
METAL 44 44 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 44 44 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 161 161 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 275 275 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 286 286 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 288 288 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
BINDING 48 48 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 182 182 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 291 291 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 336 336 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 371 371 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 376 376 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 478 478 5-amino-6-(D-ribitylamino)uracil.
{ECO:0000256|HAMAP-Rule:MF_00178}.
BINDING 566 566 5-amino-6-(D-ribitylamino)uracil; via
amide nitrogen and carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00178}.
BINDING 580 580 1-deoxy-L-glycero-tetrulose 4-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00178}.
SITE 144 144 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 182 182 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SEQUENCE 613 AA; 65409 MW; 5819031C540B567B CRC64;
MSAGHDSYRP GPAEERLVLD PVEQAVADIA AGRPVVVVDD EDRENEGDLV LAAEKATPEV
VAFMMSECRG LICAPLEGPD LDRLDLPQMV ATNTESMQTA FTVSVDGSAA HGVTTGISAA
DRATTLRLLA HATTTAGDLV RPGHVFPLRA KPGGVLVRPG HTEAAVDLAR LAGLRPAGAI
VEIAGEDGTM LRLPELVPFA RKHGLSIISI EDLIAYRRSS EPTVRREATV RLPTASGDFT
AYGYRSTVDG VEHVALVHGD LGDGEDVLVR LHSECLTGDI FHSQRCDCGP QLQKSMDRVV
EDGRGVVVYL RGHEGRGIGL LSKLRAYELQ ELGRDTLDAN TELGLPADAR DYAAGAQILT
DLGVRSLRLL TNNPDKSAAL TRHGLRVTGR EPLPVQAGEH NLRYLRTKRD RMGHDLPWLE
GRPPAPPDPA ATSSTYVTRH PPRPRHDHEE KRVSGKGAPE LSVKNCQDLR VAVIAAQWHE
QVMDGLVDGA LRALGELGIS EPTLLRVPGS FELPVVAKVL ASRGYDAIVA LGVVIRGGTP
HFEYVCQGVT QGLTQVSVDT GVPVGFGVLT CDTEEQALDR AGIAGSSEDK GHEAVTAAVA
TAAALRTVAE PWR


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