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Database: UniProt/TrEMBL
Entry: A2BWM1_PROM5
LinkDB: A2BWM1_PROM5
Original site: A2BWM1_PROM5 
ID   A2BWM1_PROM5            Unreviewed;       577 AA.
AC   A2BWM1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   19-FEB-2014, entry version 53.
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. 3:2515-2528(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; LMVDRNT; -.
DR   OrthoDB; EOG679TK8; -.
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:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-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; SSF55821; 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
//
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