(data stored in ACNUC7421 zone)

SWISSPROT: C3MHI9_SINFN

ID   C3MHI9_SINFN            Unreviewed;       366 AA.
AC   C3MHI9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180};
DE            EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_00180};
GN   Name=ribA {ECO:0000313|EMBL:ACP24317.1};
GN   Synonyms=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN   OrderedLocusNames=NGR_c05210 {ECO:0000313|EMBL:ACP24317.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24317.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24317.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|SAAS:SAAS00638573}.
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00180, ECO:0000256|SAAS:SAAS00638564}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00180};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00180};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_00180};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00638557};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC       hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00180,
CC       ECO:0000256|SAAS:SAAS00638520}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP
CC       synthase family. {ECO:0000256|SAAS:SAAS00534513}.
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DR   EMBL; CP001389; ACP24317.1; -; Genomic_DNA.
DR   RefSeq; WP_012707102.1; NC_012587.1.
DR   RefSeq; YP_002825070.1; NC_012587.1.
DR   STRING; 394.NGR_c05210; -.
DR   EnsemblBacteria; ACP24317; ACP24317; NGR_c05210.
DR   GeneID; 7791747; -.
DR   KEGG; rhi:NGR_c05210; -.
DR   PATRIC; fig|394.7.peg.3334; -.
DR   eggNOG; ENOG4105C66; Bacteria.
DR   eggNOG; COG0108; LUCA.
DR   eggNOG; COG0807; LUCA.
DR   HOGENOM; HOG000115440; -.
DR   KO; K14652; -.
DR   OMA; GCTTGIS; -.
DR   OrthoDB; POG091H008U; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.870.10; -; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; SSF142695; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHI9.
DR   SWISS-2DPAGE; C3MHI9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000313|EMBL:ACP24317.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00180,
KW   ECO:0000256|SAAS:SAAS00638570};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00180,
KW   ECO:0000256|SAAS:SAAS00638563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00180,
KW   ECO:0000256|SAAS:SAAS00738094}.
FT   DOMAIN      213    361       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
FT   REGION       29     30       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00180}.
FT   REGION      142    146       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00180}.
FT   METAL        30     30       Magnesium or manganese 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   METAL        30     30       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   METAL       145    145       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   BINDING      34     34       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00180}.
FT   BINDING     166    166       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00180}.
FT   SITE        128    128       Essential for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   SITE        166    166       Essential for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
SQ   SEQUENCE   366 AA;  39738 MW;  8CED1A9D10859A24 CRC64;
     MSYDQKRVVE AIRAFEAGEI VVVTDDGGRE NEGDLIVAAV HCTSEKMAFI VRHTSGIVCA
     PMPRDEAKRL NLNAMVAEND SAHTTAFTVS VDFKHGTTTG ISADDRTLTV RNLANPNVGA
     TDFVRPGHIF PLVAREGGVL MRSGHTEAAV DLCKLASLPP IGVICELVND DGTVTRGPQV
     EAFAETHGLK QVSVADLIAY RQRKETLIEK ANSFAIETAY GRAKAHTYSL PWDPMQHLAV
     VFGDVRDGVD IPVRLHLENV GADVFGNDRQ IDEIMKRIAG EGRGVIVYLR EGSVGVGVSQ
     TARKGKHERE AHSEAQARES EWLEIGLGAQ ILKDLGITSI RLLSSRERHY VGLEGFGIKI
     AATEIL
//

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