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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)]

 A0A0P7YW86_9CYAN        Unreviewed;       605 AA.
A0A0P7YW86;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
25-OCT-2017, entry version 18.
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=ribB-ribA {ECO:0000313|EMBL:KPQ35020.1};
Synonyms=ribBA {ECO:0000256|HAMAP-Rule:MF_01283};
ORFNames=HLUCCA11_12685 {ECO:0000313|EMBL:KPQ35020.1};
Phormidesmis priestleyi Ana.
Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
Phormidesmis.
NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ35020.1, ECO:0000313|Proteomes:UP000050465};
[1] {ECO:0000313|EMBL:KPQ35020.1, ECO:0000313|Proteomes:UP000050465}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ana {ECO:0000313|EMBL:KPQ35020.1};
Nelson W.C., Romine M.F., Lindemann S.R.;
"Identification and resolution of microdiversity through metagenomic
sequencing of parallel consortia.";
Submitted (SEP-2015) 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}.
-!- 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:KPQ35020.1}.
-----------------------------------------------------------------------
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EMBL; LJZR01000015; KPQ35020.1; -; Genomic_DNA.
EnsemblBacteria; KPQ35020; KPQ35020; HLUCCA11_12685.
PATRIC; fig|1666911.3.peg.4693; -.
UniPathway; UPA00275; UER00399.
UniPathway; UPA00275; UER00400.
Proteomes; UP000050465; 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:UP000050465};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00711691};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000313|EMBL:KPQ35020.1};
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:UP000050465};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283,
ECO:0000256|SAAS:SAAS00738094};
Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}.
DOMAIN 251 416 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
NP_BIND 295 299 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
NP_BIND 338 340 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 1 242 DHBP synthase. {ECO:0000256|HAMAP-
Rule:MF_01283}.
REGION 63 64 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 181 185 D-ribulose 5-phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01283}.
REGION 243 605 GTP cyclohydrolase II.
{ECO:0000256|HAMAP-Rule:MF_01283}.
ACT_SITE 372 372 Proton acceptor; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
ACT_SITE 374 374 Nucleophile; for GTP cyclohydrolase
activity. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 64 64 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 64 64 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 184 184 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_01283}.
METAL 300 300 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 311 311 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
METAL 313 313 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01283}.
BINDING 68 68 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 205 205 D-ribulose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 316 316 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 360 360 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 395 395 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
BINDING 400 400 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 167 167 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SITE 205 205 Essential for DHBP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_01283}.
SEQUENCE 605 AA; 67009 MW; CB54CE0AAABE875F CRC64;
MVDAASAISD QNAKDQNANE FIAEGADLFR QNPDQAFEFD SIESALADLA AGRAIVVVDD
EDRENEGDVI CAAQFATPDM INFMAVEARG LICLAMTGDR LDELDLPLMV TSSPFEDENE
QTAFTVSIDA STQLGVTTGI SAEDRARTIQ VAINSEAKPQ DLRRPGHIFP LRAKAGGVLK
RVGHTEAGVD LARLAGLYPA AVICEISNPD GSMARRPDLV GYAQRHGLKF ISIADLISYR
LRHERIVKRE AVAEMPTKFG EFKVYAYRNE LDGSEHIALV KGDPETFKSE PVMVRMHSEC
LTGDALGSLR CDCRMQLQAA LKMIESAGKG VVVYLRQEGR GIGLVNKLKA YSLQDMGLDT
VEANERLGLP VDQRNYGMGA QILMDLGVSQ FRLITNNPRK IAGLKGYGLE MVDRLPLLIE
ATTYNASYLA TKAQKLGHML LQTYLVTVAI HWREEISHSE EEATTARYER LERLRNLGQR
HNLITQEEAR SVAVAVFGQM PLIAHLGLDQ ANLADPCWYT DPEHPYVQAV ASLLDELIAW
KDIDQLEFLI SDGGDPFTQL KVKLDQQRFS WPTENRQSVM PSGVCQGLET QRIYVFSQHQ
GFSPH


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