ID   Y6440_STRCO             Reviewed;         250 AA.
AC   Q9ZBH3;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Putative (5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000250|UniProtKB:Q58499};
DE            EC=4.2.3.153 {ECO:0000250|UniProtKB:Q58499};
DE   AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000250|UniProtKB:Q58499};
DE            Short=4-HFC-P synthase {ECO:0000250|UniProtKB:Q58499};
GN   OrderedLocusNames=SCO6440; ORFNames=SC9B5.07;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the formation of 4-(hydroxymethyl)-2-
CC       furancarboxaldehyde phosphate (4-HFC-P) from two molecules of
CC       glyceraldehyde-3-P (GA-3-P). {ECO:0000250|UniProtKB:Q58499}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-
CC         furancarboxaldehyde phosphate + 2 H2O + phosphate;
CC         Xref=Rhea:RHEA:43536, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:83407; EC=4.2.3.153;
CC         Evidence={ECO:0000250|UniProtKB:Q58499};
CC   -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000305}.
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DR   EMBL; AL939127; CAA22749.1; -; Genomic_DNA.
DR   PIR; T35927; T35927.
DR   RefSeq; NP_630525.1; NC_003888.3.
DR   RefSeq; WP_003972538.1; NZ_VNID01000002.1.
DR   AlphaFoldDB; Q9ZBH3; -.
DR   SMR; Q9ZBH3; -.
DR   STRING; 100226.SCO6440; -.
DR   GeneID; 1101879; -.
DR   KEGG; sco:SCO6440; -.
DR   PATRIC; fig|100226.15.peg.6540; -.
DR   eggNOG; COG1891; Bacteria.
DR   HOGENOM; CLU_068659_0_0_11; -.
DR   InParanoid; Q9ZBH3; -.
DR   OMA; NFPWVIR; -.
DR   PhylomeDB; Q9ZBH3; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007565; 4HFCP_synth.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF04476; 4HFCP_synth; 1.
DR   PIRSF; PIRSF015957; UCP015957; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..250
FT                   /note="Putative (5-formylfuran-3-yl)methyl phosphate
FT                   synthase"
FT                   /id="PRO_0000134871"
FT   ACT_SITE        29
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q58499"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q58499"
SQ   SEQUENCE   250 AA;  26177 MW;  1A249A6F2AE72F3F CRC64;
     MLLLISPDGV DEALDCAKAA EHLDIVDVKK PDEGSLGANY PWVIREIRAA VPADKPVSAT
     VGDVPYKPGT VAQAALGAAV SGATYIKVGL YGCATPEQAV EVMRGVVRAV KDHRADAFVV
     ASGYADAHRI GCVNPLSLPD IARRSGSDAA MLDTAIKDGT RLFDHVPPDV CAEFVRRAHD
     CGLLAALAGS VRSGDLGELA RIQTDIVGVR GAVCEGGDRT TGRIRPHLVA AFRAEMDRHV
     REHAAAAAQS