ID D2QU60_SPILD Unreviewed; 432 AA.
AC D2QU60;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 29-MAY-2013, entry version 28.
DE RecName: Full=Riboflavin biosynthesis protein RibBA;
GN Name=ribBA; OrderedLocusNames=Slin_6384;
OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Spirosoma.
OX NCBI_TaxID=504472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA Goker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Spirosoma linguale DSM 74.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC pyrophosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC dihydroxybutan-2-one 4-phosphate.
CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC 1/1.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC 6-(D-ribitylamino)uracil from GTP: step 1/4.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC cyclohydrolase II family.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP
CC synthase family.
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DR EMBL; CP001769; ADB42342.1; -; Genomic_DNA.
DR RefSeq; YP_003391141.1; NC_013730.1.
DR EnsemblBacteria; ADB42342; ADB42342; Slin_6384.
DR GeneID; 8730168; -.
DR KEGG; sli:Slin_6384; -.
DR PATRIC; 32442695; VBISpiLin97822_6349.
DR HOGENOM; HOG000115440; -.
DR KO; K14652; -.
DR OMA; NIDPFIS; -.
DR BioCyc; SLIN504472:GHKB-6441-MONOMER; -.
DR UniPathway; UPA00275; UER00399.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:HAMAP.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.90.870.10; -; 1.
DR HAMAP; MF_00179; RibA; 1; -.
DR HAMAP; MF_00180; RibB; 1; -.
DR HAMAP; MF_01283; RibBA; 1; -.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
DR InterPro; IPR000926; GTP_CycHdrlaseII_RibA.
DR InterPro; IPR016299; Riboflavin_synth_RibBA.
DR Pfam; PF00926; DHBP_synthase; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR PIRSF; PIRSF001259; RibA; 1.
DR SUPFAM; SSF55821; DHBP_synth_RibB-like_a/b_dom; 1.
DR TIGRFAMs; TIGR00505; ribA; 1.
DR TIGRFAMs; TIGR00506; ribB; 1.
PE 3: Inferred from homology;
KW Complete proteome; GTP-binding; Hydrolase; Lyase; Magnesium;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Riboflavin biosynthesis; Zinc.
FT NP_BIND 277 281 GTP (By similarity).
FT NP_BIND 320 322 GTP (By similarity).
FT REGION 1 226 DHBP synthase (By similarity).
FT REGION 51 52 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 165 169 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 227 432 GTP cyclohydrolase II (By similarity).
FT ACT_SITE 354 354 Proton acceptor; for GTP cyclohydrolase
FT activity (By similarity).
FT ACT_SITE 356 356 Nucleophile; for GTP cyclohydrolase
FT activity (By similarity).
FT METAL 52 52 Magnesium or manganese 1 (By similarity).
FT METAL 52 52 Magnesium or manganese 2 (By similarity).
FT METAL 168 168 Magnesium or manganese 2 (By similarity).
FT METAL 282 282 Zinc; catalytic (By similarity).
FT METAL 293 293 Zinc; catalytic (By similarity).
FT METAL 295 295 Zinc; catalytic (By similarity).
FT BINDING 56 56 D-ribulose 5-phosphate (By similarity).
FT BINDING 189 189 D-ribulose 5-phosphate (By similarity).
FT BINDING 298 298 GTP (By similarity).
FT BINDING 342 342 GTP (By similarity).
FT BINDING 377 377 GTP (By similarity).
FT BINDING 382 382 GTP (By similarity).
FT SITE 151 151 Essential for DHBP synthase activity (By
FT similarity).
FT SITE 189 189 Essential for DHBP synthase activity (By
FT similarity).
SQ SEQUENCE 432 AA; 47621 MW; 2103DF9F08ED4892 CRC64;
MMSNNSTNSE INSANEENPA ESNPIRLDRI EDAIADIKAG KIVLVVDDED RENEGDMICA
AEMITPEMVN FMVREARGLM CAPLTQERCD ELGLDMMVTS NTSVHTTPFT VSVDLLGNGC
TTGISASDRS KTIQALVDPN TTPDDLGRPG HIFPLRAVEG GVIRRAGHTE AAVDLAKLAG
LSPVGVLIEV LNEDGTMARL PELRVLADRF GMRLVSIQDL IAYRLRTETL IRREIGVDMP
TQWGHFDLIA YKQSNTGDTH LALVKGTWEP NEPVMVRVHS SCVTGDIFGS CRCDCGPQLH
AAMELVEKEG KGVVVYMFQE GRGIGLINKL KAYKLQEMGR DTVEANLDLG LPMDARDYGV
GAQILRDLGI RKLRLISNNP KKRAGLMGYG LEIVDTVPLE IKSNPHNERY LRTKRDKMGH
TIMNEPVNEE QE
//