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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)]

 W5YD91_KOMXY            Unreviewed;       421 AA.
W5YD91;
16-APR-2014, integrated into UniProtKB/TrEMBL.
16-APR-2014, sequence version 1.
18-JUL-2018, entry version 39.
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=H845_3210 {ECO:0000313|EMBL:AHI27111.1};
Komagataeibacter xylinus E25.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
Acetobacteraceae; Komagataeibacter.
NCBI_TaxID=1296990 {ECO:0000313|EMBL:AHI27111.1, ECO:0000313|Proteomes:UP000019231};
[1] {ECO:0000313|EMBL:AHI27111.1, ECO:0000313|Proteomes:UP000019231}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=E25 {ECO:0000313|EMBL:AHI27111.1,
ECO:0000313|Proteomes:UP000019231};
Kubiak K., Kurzawa M., Jedrzejczak-Krzepkowska M., Krystynowicz A.,
Krawczyk M., Migdalski A., Kacprzak M., Loska D., Bielecki S.;
Submitted (FEB-2013) 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_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: D-ribulose 5-phosphate = formate + L-3,4-
dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
-!- 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_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};
-!- 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|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}.
-----------------------------------------------------------------------
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EMBL; CP004360; AHI27111.1; -; Genomic_DNA.
EnsemblBacteria; AHI27111; AHI27111; H845_3210.
KEGG; gxl:H845_3210; -.
PATRIC; fig|1296990.3.peg.3458; -.
KO; K14652; -.
UniPathway; UPA00275; UER00399.
UniPathway; UPA00275; UER00400.
Proteomes; UP000019231; 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; 3.40.50.10990; -; 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:UP000019231};
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:AHI27111.1};
Lyase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000313|EMBL:AHI27111.1};
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};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00179,
ECO:0000256|SAAS:SAAS00037880};
Zinc {ECO:0000256|HAMAP-Rule:MF_00179, ECO:0000256|SAAS:SAAS00711685}.
DOMAIN 220 388 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
NP_BIND 266 270 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
NP_BIND 310 312 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
REGION 31 32 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
REGION 144 148 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
ACT_SITE 344 344 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00179}.
ACT_SITE 346 346 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00179}.
METAL 32 32 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 32 32 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 147 147 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 271 271 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00179}.
METAL 282 282 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00179}.
METAL 284 284 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00179}.
BINDING 36 36 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
BINDING 168 168 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
BINDING 287 287 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
BINDING 332 332 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
BINDING 367 367 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
BINDING 372 372 GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
SITE 130 130 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SITE 168 168 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SEQUENCE 421 AA; 45249 MW; 68B2A588177E0621 CRC64;
MSVSLMPPAL AQAVATIRRG GMIILVDDED RENEGDLVMA AELMTPAAMN FMVTHARGLV
CMPMSPERIA QLNLPMMTQV NTCPRGTAFT VSIEAREGVT TGISAADRAE TVLVAAAPDA
KPADLVSPGH IFPLRAVPGG TVVRPGHTEA SVDLARMAGL IPAAVICEIM NDDGTMARMD
DLRPYARRHG LQILSIAELA KWLEANPIDA TPEARPAIEQ VARAHLPSRF GGPDMMIHAF
RAPDGTEHVA MVKGQPDRAG AVPLVRLHSE CVTGDALGSL RCDCGAQLQG ALERIGRAES
GVLVYVRGHE GRGIGLANKI RAYALQDEGL DTVDANHRLG FQTDARDWQA ASAILRALGV
NRLDLLTNNP DKVRALERHG FDVRERIPLA VEPNPFNRAY LEAKRTRMGH ALCEPVTADA
H


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