(data stored in ACNUC7421 zone)

SWISSPROT: A1AYH4_PARDP

ID   A1AYH4_PARDP            Unreviewed;       223 AA.
AC   A1AYH4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|RuleBase:RU003843};
DE            Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE            EC=4.1.99.12 {ECO:0000256|RuleBase:RU003843};
GN   OrderedLocusNames=Pden_0204 {ECO:0000313|EMBL:ABL68318.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68318.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|RuleBase:RU003843, ECO:0000256|SAAS:SAAS00357067}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl
CC         phosphate + formate + H(+); Xref=Rhea:RHEA:18457,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58121,
CC         ChEBI:CHEBI:58830; EC=4.1.99.12;
CC         Evidence={ECO:0000256|RuleBase:RU003843,
CC         ECO:0000256|SAAS:SAAS01120078};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|RuleBase:RU003843};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00608866};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC       hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC       1/1. {ECO:0000256|RuleBase:RU003843,
CC       ECO:0000256|SAAS:SAAS00317950}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003843,
CC       ECO:0000256|SAAS:SAAS00434290}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
CC       {ECO:0000256|RuleBase:RU003843, ECO:0000256|SAAS:SAAS00548340}.
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DR   EMBL; CP000489; ABL68318.1; -; Genomic_DNA.
DR   RefSeq; WP_011746551.1; NC_008686.1.
DR   STRING; 318586.Pden_0204; -.
DR   PRIDE; A1AYH4; -.
DR   EnsemblBacteria; ABL68318; ABL68318; Pden_0204.
DR   KEGG; pde:Pden_0204; -.
DR   eggNOG; ENOG4105C66; Bacteria.
DR   eggNOG; COG0108; LUCA.
DR   HOGENOM; HOG000115444; -.
DR   KO; K14652; -.
DR   OMA; VVCEMLD; -.
DR   BioCyc; PDEN318586:G1GW1-201-MONOMER; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
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;
DR   PRODOM; A1AYH4.
DR   SWISS-2DPAGE; A1AYH4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Lyase {ECO:0000256|RuleBase:RU003843, ECO:0000256|SAAS:SAAS00183995};
KW   Magnesium {ECO:0000256|RuleBase:RU003843,
KW   ECO:0000256|SAAS:SAAS00317983};
KW   Manganese {ECO:0000256|RuleBase:RU003843,
KW   ECO:0000256|SAAS:SAAS00434696};
KW   Metal-binding {ECO:0000256|RuleBase:RU003843,
KW   ECO:0000256|SAAS:SAAS00434439};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Riboflavin biosynthesis {ECO:0000256|RuleBase:RU003843,
KW   ECO:0000256|SAAS:SAAS00434473}.
SQ   SEQUENCE   223 AA;  23642 MW;  C190312894CC7956 CRC64;
     MNIETVIRAS EPELHSQDQQ PGDRVGMAID IIAAGGMVIV VDDDSRENEG DLIASAETIT
     PQMVAFMVNH STGILCASMS GARADALHLP PMVTRNDDPQ GTAYTVSCDA AACGTGVSAA
     DRTLSFHALA AGATDPAALR RPGHIFPLRA REGGVLTREG HTEAAFDLVR LAGHLPVGVL
     CELVNRDGTM MAGPQIDRFA ERHGLLKVSV AELIAWRRQR GDL
//

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