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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)]

 J8B8E0_BACCE            Unreviewed;       397 AA.
J8B8E0;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
25-OCT-2017, entry version 42.
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};
ORFNames=IEE_01323 {ECO:0000313|EMBL:EJQ47319.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ47319.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ47319.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ47319.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJQ47319.1}.
-----------------------------------------------------------------------
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EMBL; AHDJ01000018; EJQ47319.1; -; Genomic_DNA.
RefSeq; WP_002199421.1; NZ_JH791996.1.
EnsemblBacteria; EJQ47319; EJQ47319; IEE_01323.
PATRIC; fig|1053189.3.peg.1345; -.
UniPathway; UPA00275; UER00399.
UniPathway; UPA00275; UER00400.
Proteomes; UP000006600; Unassembled WGS sequence.
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:UP000006600};
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};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00738094};
Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}.
DOMAIN 206 371 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
NP_BIND 250 254 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
NP_BIND 293 295 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 1 199 DHBP synthase. {ECO:0000256|HAMAP-
Rule:MF_01283}.
REGION 26 27 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 138 142 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 200 397 GTP cyclohydrolase II.
{ECO:0000256|HAMAP-Rule:MF_01283}.
ACT_SITE 327 327 Proton acceptor; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
ACT_SITE 329 329 Nucleophile; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 27 27 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 27 27 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 141 141 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 255 255 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 266 266 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 268 268 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
BINDING 31 31 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 162 162 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 271 271 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 315 315 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 350 350 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 355 355 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 124 124 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 162 162 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SEQUENCE 397 AA; 44041 MW; 732670DC951F45E0 CRC64;
MFHRIEEALK DLKQGKVVIV CDDENRENEG DFIALAEYIT PETINFMITH GRGLVCVPIT
EQYAERLQLE PMVSHNTDSH HTAFTVSIDH VSTTTGISAH ERATTIQELL NPASKGTDFN
RPGHIFPLIA KEGGVLRRAG HTEAAVDLAK LCGTEPAGVI CEIINEDGTM ARVPDLIQCA
KQFDIKMITI EDLIAYRRHH ETLVTREVEI TLPTDFGTFH AIGYSNSLDM KEHIALVKGD
VSTGEPVLVR VHSECLTGDV FGSCRCDCGP QLHAALAQIE REGKGVLLYM RQEGRGIGLL
NKLRAYKLQE EGFDTVEANE KLGFPADLRD YGIGAQILKD LGLQSLRLLT NNPRKIAGLQ
GYDLEVTERV PLQMPAKEEN KTYLQTKVNK LGHLLNL


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