(data stored in ACNUC7421 zone)

HOGENOM: CHLTB_1_PE100

ID   CHLTB_1_PE100                        STANDARD;      PRT;   424 AA.
AC   CHLTB_1_PE100; B0BAI6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Riboflavin biosynthesis protein ribBA; (CHLTB_1.PE100).
GN   Name=ribA; Synonyms=ribBA; OrderedLocusNames=CTLon_0100;
OS   CHLAMYDIA TRACHOMATIS L2B/UCH-1/PROCTITIS.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLTB_1.PE100.
CC       Chlamydia trachomatis L2b/UCH-1/proctitis, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B0BAI6_CHLTB
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.
CC   -!- GENE_FAMILY: HOG000115440 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0BAI6; -.
DR   EMBL; AM884177; CAP06498.1; -; Genomic_DNA.
DR   RefSeq; YP_001653203.1; NC_010280.1.
DR   ProteinModelPortal; B0BAI6; -.
DR   STRING; B0BAI6; -.
DR   GeneID; 5859088; -.
DR   GenomeReviews; AM884177_GR; CTLon_0100.
DR   KEGG; ctl:CTLon_0100; -.
DR   OMA; RCDCRMQ; -.
DR   ProtClustDB; PRK09311; -.
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   HAMAP; MF_00179; RibA; 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   Gene3D; G3DSA:3.90.870.10; DHBP_synth_RibB-like_a/b_dom; 1.
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.
DR   HOGENOMDNA; CHLTB_1.PE100; -.
KW   Complete proteome; GTP-binding; Hydrolase; Lyase; Magnesium;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Riboflavin biosynthesis; Zinc.
SQ   SEQUENCE   424 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MFTYEAGIAS VQQAIKDVAE GKFVIVIDAA SRENEGDLIL AGEKVSTEKM SFLLSHTTGI
     VCASLSREQA KSLDLPAMVQ DNQCAFKTAF TVSVDASSGV TTGVSASDRT RTVQLLADPA
     ATAESFVRPG HVFPLISQPG GVVQRPGHTE AAMDLMRLAG MQPCGIFAEL VNPDHSMMRQ
     QQVLAFAEQH DLTVITVDDL ITYRYTYDSL VTKISSARLP TKYGDFSIYV YESIIDGTQH
     FALVKGDIHE QEAVPVRVHS ECLTGDILGS CRCDCGAQLD MAMRYIAEEG LGVIVYLRGQ
     EGRGIGFGHK IRAYALQDLG YDTVDANLQL GFPIDAREYG MAAQVLKDLQ LTSVRLITHN
     PRKFFELQRL GIHVLDRIIL PVSISTENEG YLRTKKERMG HWLDLPVLDD VEEEYETVER
     MSCR
//

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