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Multifunctional fusion protein [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)]

 R0EBK1_CAUVI            Unreviewed;       392 AA.
R0EBK1;
26-JUN-2013, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 1.
05-DEC-2018, entry version 46.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00179, ECO:0000256|HAMAP-Rule:MF_00180};
Includes:
RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_00179};
EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_00179};
AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_00179};
Includes:
RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00180};
Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180};
EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_00180};
Name=ribA {ECO:0000256|HAMAP-Rule:MF_00179};
Synonyms=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
ORFNames=OR37_01047 {ECO:0000313|EMBL:ENZ82853.1};
Caulobacter vibrioides OR37.
Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
Caulobacteraceae; Caulobacter.
NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ82853.1, ECO:0000313|Proteomes:UP000013063};
[1] {ECO:0000313|EMBL:ENZ82853.1, ECO:0000313|Proteomes:UP000013063}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR37 {ECO:0000313|EMBL:ENZ82853.1,
ECO:0000313|Proteomes:UP000013063};
PubMed=23792749;
Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M.,
Epstein S.E., Palumbo A.V., Brown S.D.;
"Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
Tolerant to Heavy Metals.";
Genome Announc. 1:0-0(2013).
-!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
formate and 3,4-dihydroxy-2-butanone 4-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00180}.
-!- 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_00179}.
-!- 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_00180};
-!- 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_00179,
ECO:0000256|SAAS:SAAS00711742};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
Note=Binds 2 divalent metal cations per subunit. Magnesium or
manganese. {ECO:0000256|HAMAP-Rule:MF_00180};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_00179};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00179};
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
1/1. {ECO:0000256|HAMAP-Rule:MF_00180}.
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|HAMAP-
Rule:MF_00179, ECO:0000256|SAAS:SAAS00711724}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}.
-!- SIMILARITY: Belongs to the DHBP synthase family.
{ECO:0000256|HAMAP-Rule:MF_00180}.
-!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
{ECO:0000256|HAMAP-Rule:MF_00179}.
-!- SIMILARITY: In the C-terminal section; belongs to the GTP
cyclohydrolase II family. {ECO:0000256|SAAS:SAAS00789992}.
-!- SIMILARITY: In the N-terminal section; belongs to the DHBP
synthase family. {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:ENZ82853.1}.
-----------------------------------------------------------------------
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EMBL; APMP01000004; ENZ82853.1; -; Genomic_DNA.
RefSeq; WP_004616631.1; NZ_APMP01000004.1.
EnsemblBacteria; ENZ82853; ENZ82853; OR37_01047.
PATRIC; fig|1292034.3.peg.1032; -.
OrthoDB; POG091H008U; -.
UniPathway; UPA00275; UER00399.
UniPathway; UPA00275; UER00400.
Proteomes; UP000013063; 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; 3.40.50.10990; -; 1.
HAMAP; MF_00179; RibA; 1.
HAMAP; MF_00180; RibB; 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.
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:UP000013063};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_00179,
ECO:0000256|SAAS:SAAS00711691};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00179,
ECO:0000256|SAAS:SAAS01033620, ECO:0000313|EMBL:ENZ82853.1};
Lyase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000313|EMBL:ENZ82853.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00180};
Manganese {ECO:0000256|HAMAP-Rule:MF_00180};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00179,
ECO:0000256|SAAS:SAAS00037896};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00179,
ECO:0000256|SAAS:SAAS00711691};
Reference proteome {ECO:0000313|Proteomes:UP000013063};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00179,
ECO:0000256|SAAS:SAAS00037880};
Zinc {ECO:0000256|HAMAP-Rule:MF_00179, ECO:0000256|SAAS:SAAS00711685}.
DOMAIN 203 364 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
NP_BIND 243 247 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
NP_BIND 286 288 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
REGION 25 26 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
REGION 138 142 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
ACT_SITE 320 320 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00179}.
ACT_SITE 322 322 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00179}.
METAL 26 26 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 26 26 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 141 141 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 248 248 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00179}.
METAL 259 259 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00179}.
METAL 261 261 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00179}.
BINDING 30 30 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
BINDING 162 162 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
BINDING 264 264 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
BINDING 308 308 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
BINDING 343 343 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
BINDING 348 348 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
SITE 124 124 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SITE 162 162 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SEQUENCE 392 AA; 41072 MW; 6E323DC7317E89A1 CRC64;
MSRLSEALER LKAGGMIIVV DDIDRENEGD LVMAAEHVDA AAIAFMAKEG SGLICLSLEA
QAVERLNLAP MVADNRTRRG TAFTVSIEAA VGIDTGISAH DRAMTIAAAT APDATAADLV
SPGHVFPLRA APGGVLVRRG HTEASIDLVT LAGLRPAAVI CEIMNPDGAM ARGPSLDAFA
ARHGLPVVSI AELVEHRRAV TEVARANLPT EHGTFEVVAF RTQDAEHLAL IAAPRDGAAP
LVRVHSECLT GDALGSRRCD CGEQLRASLD RIGQDGGVLV YVGGHEGRGL GLANKIAAYA
LQDQGLDTVS ANHALGFVDD ARDYGAAGQI LQALGVGRVR LMTNNPRKVE AMTAAGLEVV
ERVPVLVRQT DDNAAYLTTK RDRLGHDLGH AA


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