ID A1SJG8_NOCSJ Unreviewed; 426 AA.
AC A1SJG8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 01-MAY-2013, entry version 50.
DE RecName: Full=Riboflavin biosynthesis protein RibBA;
GN Name=ribBA; OrderedLocusNames=Noca_2449;
OS Nocardioides sp. (strain BAA-499 / JS614).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Propionibacterineae; Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Mattes T., Gossett J., Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) 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; CP000509; ABL81953.1; -; Genomic_DNA.
DR RefSeq; YP_923640.1; NC_008699.1.
DR ProteinModelPortal; A1SJG8; -.
DR SMR; A1SJG8; 209-380.
DR STRING; 196162.Noca_2449; -.
DR EnsemblBacteria; ABL81953; ABL81953; Noca_2449.
DR GeneID; 4599790; -.
DR KEGG; nca:Noca_2449; -.
DR PATRIC; 22746929; VBINocSp122728_2704.
DR eggNOG; COG0108; -.
DR HOGENOM; HOG000115440; -.
DR KO; K14652; -.
DR OMA; VIERIPI; -.
DR ProtClustDB; CLSK2783565; -.
DR BioCyc; NSP196162:GH4V-2504-MONOMER; -.
DR UniPathway; UPA00275; UER00399.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
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 256 260 GTP (By similarity).
FT NP_BIND 300 302 GTP (By similarity).
FT REGION 1 205 DHBP synthase (By similarity).
FT REGION 31 32 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 144 148 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 206 426 GTP cyclohydrolase II (By similarity).
FT ACT_SITE 334 334 Proton acceptor; for GTP cyclohydrolase
FT activity (By similarity).
FT ACT_SITE 336 336 Nucleophile; for GTP cyclohydrolase
FT activity (By similarity).
FT METAL 32 32 Magnesium or manganese 1 (By similarity).
FT METAL 32 32 Magnesium or manganese 2 (By similarity).
FT METAL 147 147 Magnesium or manganese 2 (By similarity).
FT METAL 261 261 Zinc; catalytic (By similarity).
FT METAL 272 272 Zinc; catalytic (By similarity).
FT METAL 274 274 Zinc; catalytic (By similarity).
FT BINDING 36 36 D-ribulose 5-phosphate (By similarity).
FT BINDING 168 168 D-ribulose 5-phosphate (By similarity).
FT BINDING 277 277 GTP (By similarity).
FT BINDING 322 322 GTP (By similarity).
FT BINDING 357 357 GTP (By similarity).
FT BINDING 362 362 GTP (By similarity).
FT SITE 130 130 Essential for DHBP synthase activity (By
FT similarity).
FT SITE 168 168 Essential for DHBP synthase activity (By
FT similarity).
SQ SEQUENCE 426 AA; 46321 MW; 37F86CBDB3BEB159 CRC64;
MSTEIRLDTV ERAIADIAAG KAVVVVDDED RENEGDIIFA ASKATPDLMA FTIRYSSGVI
CVPMPARMLD RLEIPLMTPH NKDRLRTAYT ISVDARDGVT TGISAADRAH TVRVLADSAT
EPWEITRPGH VFPLRYREGG VLVRRGHTEA AVDLAKLAGL TPAGVLVEVV NDDGTMKRGP
ELRAFADEHG LAMISIDDLV RYRRRHETLV ERVAETQLPT RHGDFTAYGY RITVDGSEHI
ALVHGDISGP EPVLTRVHSE CLTGDVFGSH RCDCGPQLEE ALERIVAEGR GVVVYLRGHE
GRGIGLVAKL QAYQLQDGGR DTVDANLDLG LPADARHYGT ATQVLRDLGV GSVRLMTNNP
DKVRNLEDYG VSVAARVPLT PHPNDHNIAY LLTKRDRMGH DLPNLADGVP DTRADGVPDT
LAQNGA
//
