(data stored in ACNUC7421 zone)

HOGENOM: NEIML_1_PE1009

ID   NEIML_1_PE1009                       STANDARD;      PRT;   446 AA.
AC   NEIML_1_PE1009; C6S777;
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   SubName: Full=Putative 3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE   EC=3.5.4 25; (NEIML_1.PE1009).
GN   Name=ribB; OrderedLocusNames=NMO_1070;
OS   NEISSERIA MENINGITIDIS ALPHA14.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=662598;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEIML_1.PE1009.
CC       Neisseria meningitidis alpha14, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6S777_NEIML
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate.
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   -!- GENE_FAMILY: HOG000115440 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6S777; -.
DR   EMBL; AM889136; CBA06090.1; -; Genomic_DNA.
DR   RefSeq; YP_003083258.1; NC_013016.1.
DR   EnsemblBacteria; EBNEIT00000014337; EBNEIP00000014054; EBNEIG00000014337.
DR   GeneID; 8221633; -.
DR   GenomeReviews; AM889136_GR; NMO_1070.
DR   GeneTree; EBGT00050000021391; -.
DR   OMA; IEYRSRT; -.
DR   ProtClustDB; PRK14019; -.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:HAMAP.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00180; RibB; 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; TIGR00506; RibB; 1.
DR   HOGENOMDNA; NEIML_1.PE1009; -.
KW   Complete proteome; Hydrolase; Lyase; Magnesium; Manganese;
KW   Metal-binding; Riboflavin biosynthesis.
SQ   SEQUENCE   446 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDTAGLRRR NLRQWIAEHY GGLQTRFAEA VALNTGELSA LLKNKSFGEK KARKIEQAAK
     MPAFWLDTEH TARPPEHTGK HTMSHISPIP EILADIKAGK MVIITDAEDR ENEGDLLMAA
     QFVTPEAINF MIKHARGLVC LPMDGEMVEK LGLPMMTQKN GAQYGTNFTV SIEAAHGITT
     GISAADRALT IQTAVSPTAK PEDIVQPGHI FPLRAQKGGV LVRAGHTEAG VDLAQMNGLI
     PAAVICEIIN DDGTMARMPE LMKFAEEHKL KIGTITDLIE YRSRTESLLE DMGNAPVQTP
     WGEFQQHVYV DKLSGETHLA LVKGTPAADT ETLVRVHEPF SVMDFIQANP RHSWSLPKAL
     ERIQQAESGV VILLHRAEDG ASLLDRTLPK GANQAYKWDS KSYGIGAQIL VGLNVKKLRV
     LGQPSSFTGL TGFGLEVVGF EEAENK
//

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