FAEHP_METBU
ID FAEHP_METBU Reviewed; 396 AA.
AC Q12UK3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Bifunctional enzyme Fae/Hps {ECO:0000255|HAMAP-Rule:MF_01268};
DE Includes:
DE RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase {ECO:0000255|HAMAP-Rule:MF_01268};
DE EC=4.2.1.147 {ECO:0000255|HAMAP-Rule:MF_01268};
DE AltName: Full=Formaldehyde-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01268};
DE Short=Fae {ECO:0000255|HAMAP-Rule:MF_01268};
DE Includes:
DE RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01268};
DE Short=HPS {ECO:0000255|HAMAP-Rule:MF_01268};
DE EC=4.1.2.43 {ECO:0000255|HAMAP-Rule:MF_01268};
DE AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase {ECO:0000255|HAMAP-Rule:MF_01268};
GN Name=fae-hps {ECO:0000255|HAMAP-Rule:MF_01268};
GN OrderedLocusNames=Mbur_1994;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC tetrahydromethanopterin (H(4)MPT) to 5,10-
CC methylenetetrahydromethanopterin. {ECO:0000255|HAMAP-Rule:MF_01268}.
CC -!- FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate
CC and formaldehyde from 3-hexulose-6-phosphate. {ECO:0000255|HAMAP-
CC Rule:MF_01268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-
CC methylenetetrahydromethanopterin + H2O; Xref=Rhea:RHEA:24678,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:57818,
CC ChEBI:CHEBI:58103; EC=4.2.1.147; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01268};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose
CC 6-phosphate; Xref=Rhea:RHEA:25201, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58542; EC=4.1.2.43;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01268};
CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01268}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the formaldehyde-
CC activating enzyme family. {ECO:0000255|HAMAP-Rule:MF_01268}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family.
CC HPS subfamily. {ECO:0000255|HAMAP-Rule:MF_01268}.
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DR EMBL; CP000300; ABE52873.1; -; Genomic_DNA.
DR RefSeq; WP_011500014.1; NC_007955.1.
DR AlphaFoldDB; Q12UK3; -.
DR SMR; Q12UK3; -.
DR STRING; 259564.Mbur_1994; -.
DR EnsemblBacteria; ABE52873; ABE52873; Mbur_1994.
DR GeneID; 3996946; -.
DR KEGG; mbu:Mbur_1994; -.
DR HOGENOM; CLU_701335_0_0_2; -.
DR OMA; LWDPPYL; -.
DR OrthoDB; 24053at2157; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000001979; Chromosome.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:InterPro.
DR GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04726; KGPDC_HPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.230.60; -; 1.
DR HAMAP; MF_01268; Fae_Hps; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR020868; Fae/Hps.
DR InterPro; IPR014826; HCHO-activating_enzyme.
DR InterPro; IPR037075; HCHO-activating_enzyme_sf.
DR InterPro; IPR041710; HPS/KGPDC.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF08714; Fae; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR03126; one_C_fae; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Lyase; Multifunctional enzyme; Reference proteome.
FT CHAIN 1..396
FT /note="Bifunctional enzyme Fae/Hps"
FT /id="PRO_1000067323"
FT REGION 1..161
FT /note="Formaldehyde-activating enzyme"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT REGION 162..396
FT /note="3-hexulose-6-phosphate synthase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT ACT_SITE 17
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
SQ SEQUENCE 396 AA; 42461 MW; 4EC2C5C1A4D2AB6B CRC64;
MMLIGEALIG EAPELAHVDL MIGDKEGPVG QAFATGMTQL SAGHTPVLSV IRPNLPTKPS
TLIVPKVTVK GMDQASQIFG PAQAAVSKAV ADAVEEGLIP KEKAEDLVII ASVFIHPQAV
DYNRIYRYNY GATKLALKRA LDGFPDIDTV LHEKDRAAHA VMGFKISKLW DAPYLQVALD
NPNLPVILNI IKQLPKSDHL ILEAGTPLIK RYGVDVISKI REVRPDAFIV ADLKTLDTGN
LEARMVADAT ADAIVVSALA PIATLNKVIE EAHKTGIYAV MDTLNTPDPV AVLEQLDVLP
DVVELHRAID IEGTAHAWGS IEGIKALAVK RSSKVLVAVA GGVRVDTISD ALGAGADILV
VGRAITNSKD VRQAADRFIE GLNKPEIDQF RIMTDF
