ID A2BWM1_PROM5 Unreviewed; 577 AA.
AC A2BWM1;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 29-MAY-2013, entry version 49.
DE RecName: Full=Riboflavin biosynthesis protein RibBA;
GN Name=ribB; Synonyms=ribBA; OrderedLocusNames=P9515_09751;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:E231-E231(2007).
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; CP000552; ABM72182.1; -; Genomic_DNA.
DR RefSeq; YP_001011289.1; NC_008817.1.
DR ProteinModelPortal; A2BWM1; -.
DR STRING; 167542.P9515_09751; -.
DR EnsemblBacteria; ABM72182; ABM72182; P9515_09751.
DR GeneID; 4719208; -.
DR KEGG; pmc:P9515_09751; -.
DR PATRIC; 23015552; VBIProMar113831_1001.
DR eggNOG; COG0108; -.
DR HOGENOM; HOG000115440; -.
DR KO; K14652; -.
DR OMA; LRCDCRM; -.
DR ProtClustDB; PRK09319; -.
DR BioCyc; PMAR167542:GI3N-1002-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 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 276 280 GTP (By similarity).
FT NP_BIND 319 321 GTP (By similarity).
FT REGION 1 224 DHBP synthase (By similarity).
FT REGION 48 49 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 163 167 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 225 577 GTP cyclohydrolase II (By similarity).
FT ACT_SITE 353 353 Proton acceptor; for GTP cyclohydrolase
FT activity (By similarity).
FT ACT_SITE 355 355 Nucleophile; for GTP cyclohydrolase
FT activity (By similarity).
FT METAL 49 49 Magnesium or manganese 1 (By similarity).
FT METAL 49 49 Magnesium or manganese 2 (By similarity).
FT METAL 166 166 Magnesium or manganese 2 (By similarity).
FT METAL 281 281 Zinc; catalytic (By similarity).
FT METAL 292 292 Zinc; catalytic (By similarity).
FT METAL 294 294 Zinc; catalytic (By similarity).
FT BINDING 53 53 D-ribulose 5-phosphate (By similarity).
FT BINDING 187 187 D-ribulose 5-phosphate (By similarity).
FT BINDING 297 297 GTP (By similarity).
FT BINDING 341 341 GTP (By similarity).
FT BINDING 376 376 GTP (By similarity).
FT BINDING 381 381 GTP (By similarity).
FT SITE 149 149 Essential for DHBP synthase activity (By
FT similarity).
FT SITE 187 187 Essential for DHBP synthase activity (By
FT similarity).
SQ SEQUENCE 577 AA; 64725 MW; 489D1EDC6B4EAD01 CRC64;
MKETSPKSNN GTILDNNEKF KIEFDQISDA LAAIRNGECI IVVDDERREN EGDLICAAQF
ATPQQINFMA TEGRGLICLA MQGDKLDALD LPLMVDRNTD KNQTAFTVSI DAGPENNVTT
GISAEDRAKT IQVAINPSTK PEDLRRPGHI FPLRAKKGGV LKRAGHTEAA VDIAAMSGLY
PAGVICEIQN PDGSMSRLPQ LKEYAKEWGM KLISIADLIS YRFQNERFVY RKSETILPSI
FGNFKAYGYI NDLDGSEHIA LVKQKSNKLS EPVLVRMHSE CLTGDAFGSL RCDCRPQLEA
ALSRIEKEGE GVVVYLRQEG RGIGLINKLK AYSLQDGGLD TVEANEKLGF PADLRNYGVG
AQILTDLGIK KLKLLTNNPR KIAGLGGYGI EVTERVPLVI CPGDHNAEYL NVKRQKLGHL
LEEDKINSRF VDPYIAIFLD GDYKSIDLVP IKNKTFEFCT KKNINIMLES SPRLLAFWNR
PKLVWRILHD KNREDFTIND NEIKNIEIFI KFLSEFDKSS KVGIIVSKNI EQALHPKNNI
KLKNTKFSIK NDYLYSSTRK FNLDKETFSI IFNKDLA
//
