(data stored in SCRATCH zone)

SWISSPROT: D4YXP5_SPHJU

ID   D4YXP5_SPHJU            Unreviewed;       427 AA.
AC   D4YXP5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 50.
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:BAI95127.1};
GN   Synonyms=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN   OrderedLocusNames=SJA_C1-02930 {ECO:0000313|EMBL:BAI95127.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95127.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95127.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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; AP010803; BAI95127.1; -; Genomic_DNA.
DR   RefSeq; WP_007686996.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-02930; -.
DR   EnsemblBacteria; BAI95127; BAI95127; SJA_C1-02930.
DR   GeneID; 29271996; -.
DR   KEGG; sjp:SJA_C1-02930; -.
DR   eggNOG; ENOG4105C66; Bacteria.
DR   eggNOG; COG0108; LUCA.
DR   eggNOG; COG0807; LUCA.
DR   HOGENOM; HOG000115440; -.
DR   KO; K14652; -.
DR   OMA; IEGGVHM; -.
DR   OrthoDB; POG091H008U; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YXP5.
DR   SWISS-2DPAGE; D4YXP5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Hydrolase {ECO:0000313|EMBL:BAI95127.1};
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:UP000007753};
KW   Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00180,
KW   ECO:0000256|SAAS:SAAS00738094}.
FT   DOMAIN      270    423       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
FT   REGION       89     90       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00180}.
FT   REGION      202    206       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00180}.
FT   METAL        90     90       Magnesium or manganese 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   METAL        90     90       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   METAL       205    205       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   BINDING      94     94       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00180}.
FT   BINDING     226    226       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00180}.
FT   SITE        188    188       Essential for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
FT   SITE        226    226       Essential for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00180}.
SQ   SEQUENCE   427 AA;  46286 MW;  4CB3854DEBE055CE CRC64;
     MSSALIDTVR SLVTEGGMSR SGLARAAGLH ANSLRRLGEA DWNPTAETLG KLEGYLARRE
     GGTALASPEE IINEARNGRM FILVDDEDRE NEGDLVIPAQ MATPDAINFM ATHGRGLICL
     ALSKERVDHL GLGLMSRNNG TRHETAFTVS IEAREGVTTG ISAADRARTI SVAIDGSKGR
     DDIVTPGHVF PLVAKDGGVL VRTGHTEAAV DVARLAGLNP SGVICEVMKD DGTMARLDDL
     IPFAQKHRMK IGTIRDLIAY RRRHDHMVER RAETVFNSQW GGDWKAISFY NKATQTEQLV
     LQKGHVVPDE PTLVRMHQLS LLDDVYGSTG PRNGLLARSM DIIAREGAGI IVVLTVPVPS
     DFVSRSLRHH AGQPDTGMDE LRDYGVGAQI LAELGVHDMI LLSNTHHSLI ALDGYDLAVV
     GQRPIEL
//

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