FAEHP_METMA
ID FAEHP_METMA Reviewed; 392 AA.
AC Q8PXE1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=MM_1279;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30975.1; -; Genomic_DNA.
DR RefSeq; WP_011033226.1; NC_003901.1.
DR AlphaFoldDB; Q8PXE1; -.
DR SMR; Q8PXE1; -.
DR STRING; 192952.MM_1279; -.
DR DNASU; 1479621; -.
DR EnsemblBacteria; AAM30975; AAM30975; MM_1279.
DR GeneID; 24837617; -.
DR KEGG; mma:MM_1279; -.
DR PATRIC; fig|192952.21.peg.1486; -.
DR eggNOG; arCOG00103; Archaea.
DR HOGENOM; CLU_701335_0_0_2; -.
DR OMA; LWDPPYL; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000000595; 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..392
FT /note="Bifunctional enzyme Fae/Hps"
FT /id="PRO_0000236086"
FT REGION 1..161
FT /note="Formaldehyde-activating enzyme"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT REGION 162..392
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 392 AA; 42446 MW; 50AEA625123B4039 CRC64;
MFQIGEALMG QGSELAHVDL MIGDKGGPVG QAFANGLTQL SAGHTPLLSV IRPNLPPKPS
TLIIPKVTVK NMDQAARIFG PAQSAVAKAV ADSVEEGVIP KDQVEDLVIV ASVFIHPEAQ
DYNKIYRYNY GATKLAIKRA LEGFPDIDTV LEESNKSTHA IMGFKVTRLW DPPYLQIAFD
NPNLEFVLSA ISEIPKSDHV IIEAGTPLIK RYGTDVISKI RQVRPDAFIV ADLKTLDTGN
LEARMVADAA GDAIVVSALA PISTIDKLIE EAHKTGIYAV MDTLNQQDPI SVLKQLKVMP
DVIELHRGID IEGTEHAWGN IGEIKKIAPK ALVAVAGGVR LDKVPVALSQ GADILVVGRA
ITNAKDVREM AEQFINSLNK PEIDQFRVMT DF
