ID G9PQH9_9ACTO Unreviewed; 236 AA.
AC G9PQH9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000256|ARBA:ARBA00012553};
DE EC=4.2.3.153 {ECO:0000256|ARBA:ARBA00012553};
DE AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000256|ARBA:ARBA00032523};
GN ORFNames=HMPREF0975_02650 {ECO:0000313|EMBL:EHM90752.1};
OS Actinomyces sp. oral taxon 849 str. F0330.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=653386 {ECO:0000313|EMBL:EHM90752.1, ECO:0000313|Proteomes:UP000003600};
RN [1] {ECO:0000313|EMBL:EHM90752.1, ECO:0000313|Proteomes:UP000003600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0330 {ECO:0000313|EMBL:EHM90752.1,
RC ECO:0000313|Proteomes:UP000003600};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces sp. oral taxon 849 str. F0330.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003810}.
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:0000256|ARBA:ARBA00001294};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM90752.1}.
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DR EMBL; ACTB01000173; EHM90752.1; -; Genomic_DNA.
DR RefSeq; WP_009234624.1; NZ_JH470359.1.
DR AlphaFoldDB; G9PQH9; -.
DR STRING; 653386.HMPREF0975_02650; -.
DR PATRIC; fig|653386.3.peg.2459; -.
DR eggNOG; COG1891; Bacteria.
DR HOGENOM; CLU_068659_0_0_11; -.
DR Proteomes; UP000003600; Unassembled WGS sequence.
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; Ribulose-phoshate binding barrel; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000003600};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 27
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015957-1"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015957-1"
SQ SEQUENCE 236 AA; 25153 MW; BF3798F8FE980B0B CRC64;
MRVLISPINA DEAVIAYECG TDIIDIKNTS EGSLGASFPW VIREVIERVG DPEVTFSATL
GDLPFKPGTA ALAARGAVTS GVTYIKAGLH GPKTVDEGVQ LMTAVNRAAK EVNNDVLVVT
AGYADYRRFD GLKPLQLVEI ATEAKTDLVM MDTLFKDGKT LFDSCDLAEL QEFVATAHEN
ALEVALAGSI RLQHLDQLVS IGTDIVGVRG AVCGGLNRKA TIDREKAREF MAVASA
//
