ID   Y264_KITAU              Reviewed;         251 AA.
AC   Q9X4H5;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   25-MAY-2022, entry version 51.
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};
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC   / NCIMB 8234 / A-377;
RX   PubMed=10997131; DOI=10.1007/bf02816249;
RA   Sprusansky O., Homerova D., Sevcikova B., Kormanec J.;
RT   "Cloning of the putative aldehyde dehydrogenase, aldA, gene from
RT   Streptomyces aureofaciens.";
RL   Folia Microbiol. (Praha) 44:491-502(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD23399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF110772; AAD23399.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q9X4H5; -.
DR   SMR; Q9X4H5; -.
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; Schiff base.
FT   CHAIN           1..251
FT                   /note="Putative (5-formylfuran-3-yl)methyl phosphate
FT                   synthase"
FT                   /id="PRO_0000134870"
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   251 AA;  26099 MW;  E2D53BEBE4E42801 CRC64;
     MLLLISPDSV EEALDCAKAA EHLDIVDVKK PDEGSLGANF PWVIREIRDA VPADKPVSAT
     VGDVPYKPGT VAQAALGAVV SGATYIKVGL YGCTTPDQGI EVMRAVVRAV KDHRPDALVV
     ASGYADAHRI GCVNPLAVPD IAARSGADAA MLDTAIKDGT RLFDHVPPEV CAEFVRLAHT
     SGLLAALAGS VTQADLGPLT HMGTDIVGVR GAVCEGGDRN AGRIQPHLVA AFRAEMDRHA
     REHAVGVPAV N