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Riboflavin biosynthesis protein RibBA [Includes: GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II); 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12)]

 F0S0E2_DESTD            Unreviewed;       417 AA.
F0S0E2;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
25-OCT-2017, entry version 52.
RecName: Full=Riboflavin biosynthesis protein RibBA {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=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};
Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283};
OrderedLocusNames=Dester_0009 {ECO:0000313|EMBL:ADY72670.1};
Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
Desulfurobacterium.
NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY72670.1, ECO:0000313|Proteomes:UP000007102};
[1] {ECO:0000313|Proteomes:UP000007102}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
Brambilla E., Klenk H.-P., Eisen J.A.;
"The complete genome of Desulfurobacterium thermolithotrophum DSM
11699.";
Submitted (FEB-2011) 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, ECO:0000256|SAAS:SAAS00739193}.
-!- 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}.
-!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP-
Rule:MF_01283}.
-!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
{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};
-!- 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|SAAS:SAAS00711724}.
-!- 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; CP002543; ADY72670.1; -; Genomic_DNA.
STRING; 868864.Dester_0009; -.
EnsemblBacteria; ADY72670; ADY72670; Dester_0009.
KEGG; dte:Dester_0009; -.
eggNOG; ENOG4105C66; Bacteria.
eggNOG; COG0108; LUCA.
eggNOG; COG0807; LUCA.
KO; K14652; -.
OMA; GCTTGIS; -.
OrthoDB; POG091H008U; -.
UniPathway; UPA00275; UER00399.
UniPathway; UPA00275; UER00400.
Proteomes; UP000007102; Chromosome.
GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate 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.
Gene3D; 3.90.870.10; -; 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; IPR000926; RibA.
InterPro; IPR036144; RibA-like_sf.
InterPro; IPR016299; Riboflavin_synth_RibBA.
Pfam; PF00926; DHBP_synthase; 1.
Pfam; PF00925; GTP_cyclohydro2; 1.
SUPFAM; SSF142695; SSF142695; 1.
SUPFAM; SSF55821; SSF55821; 1.
TIGRFAMs; TIGR00505; ribA; 1.
TIGRFAMs; TIGR00506; ribB; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000007102};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711691};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283};
Lyase {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711664};
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:SAAS00638563};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711691};
Reference proteome {ECO:0000313|Proteomes:UP000007102};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00738094};
Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}.
DOMAIN 215 380 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
NP_BIND 259 263 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
NP_BIND 302 304 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 1 208 DHBP synthase. {ECO:0000256|HAMAP-
Rule:MF_01283}.
REGION 32 33 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 147 151 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 209 417 GTP cyclohydrolase II.
{ECO:0000256|HAMAP-Rule:MF_01283}.
ACT_SITE 336 336 Proton acceptor; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
ACT_SITE 338 338 Nucleophile; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 33 33 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 33 33 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 150 150 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 264 264 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 275 275 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 277 277 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
BINDING 37 37 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 171 171 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 280 280 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 324 324 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 359 359 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 364 364 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 133 133 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 171 171 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SEQUENCE 417 AA; 46847 MW; 9DA98BB5B554C7C0 CRC64;
MVKGRFPLDR VEEAIEEIKK GKMVVVVDDP NRENEGDLVI AAEKVTPEAI NFMAKYGRGL
ICLALTEERC DELEIEPMTP RPTDPKETAF GISIDAHPKF GTTTGISAYD RAITIKRAID
PEAKPEDFIK PGHVFPLRAR KGGVLKRSGH TEAAVDLARL AGLYPAGVIC EIMDEDGSMM
RLPKLIDYAR KHGLKIISIA DLIEYRMKSE SLIRREAEAN LPTPYGMWKI YAYTSLVDNK
EHVALTMGEI REDEPILVRV HSECLTGDVF GSLKCDCRSQ LHKAMEMISE EGKGVIVYLR
QEGRGIGLVN KIKAYHLQDH GFDTVEANKK LGFPPDMRDF GIGAQILRDL GVKKMKLLTN
NPKKLIGLEG YGLEVVERVP IEVGICEYNI NYLKTKKEKL GHLLNLEKKE DEKYNEQ


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