位置:首页 > 蛋白库 > RIBB_SHEON
RIBB_SHEON
ID   RIBB_SHEON              Reviewed;         217 AA.
AC   Q8EKF2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_00180};
DE            EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_00180};
GN   Name=ribB {ECO:0000255|HAMAP-Rule:MF_00180}; OrderedLocusNames=SO_0142;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00180}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate +
CC         formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830;
CC         EC=4.1.99.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000255|HAMAP-Rule:MF_00180};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00180}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014299; AAN53229.1; -; Genomic_DNA.
DR   RefSeq; NP_715784.1; NC_004347.2.
DR   RefSeq; WP_011070545.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EKF2; -.
DR   SMR; Q8EKF2; -.
DR   STRING; 211586.SO_0142; -.
DR   PaxDb; Q8EKF2; -.
DR   KEGG; son:SO_0142; -.
DR   PATRIC; fig|211586.12.peg.136; -.
DR   eggNOG; COG0108; Bacteria.
DR   HOGENOM; CLU_020273_3_0_6; -.
DR   OMA; DAGGLIC; -.
DR   OrthoDB; 900513at2; -.
DR   PhylomeDB; Q8EKF2; -.
DR   BioCyc; SONE211586:G1GMP-135-MON; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Manganese; Metal-binding; Reference proteome;
KW   Riboflavin biosynthesis.
FT   CHAIN           1..217
FT                   /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT                   /id="PRO_0000151811"
FT   BINDING         37..38
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         42
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         150..154
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         174
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   SITE            136
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   SITE            174
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   217 AA;  22956 MW;  FAB54E6449441EFC CRC64;
     MNQSLLAPFG TAIERVEAGL NALRQGLGVL VVDDEDRENE GDLIFAAESL TNAQMAMLIR
     ECSGIVCLCL PDEKVKALAL PPMVENNSSQ YGTAFTVSIE AKVGVTTGVS AADRVTTIKT
     AIADHAKPSD LARPGHVYPL RAQPGGVLTR RGHTEGTIDL MQLAGLKPAG VLCEVTNPDG
     TMARLPEIIA FGALHNMPVL TIEDIVVYRK SLLANVG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024