FAEHP_METST
ID FAEHP_METST Reviewed; 406 AA.
AC Q2NE86;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Msp_1498;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57867.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NE86; -.
DR SMR; Q2NE86; -.
DR STRING; 339860.Msp_1498; -.
DR PRIDE; Q2NE86; -.
DR EnsemblBacteria; ABC57867; ABC57867; Msp_1498.
DR KEGG; mst:Msp_1498; -.
DR eggNOG; arCOG00103; Archaea.
DR HOGENOM; CLU_701335_0_0_2; -.
DR OMA; LWDPPYL; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000001931; 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..406
FT /note="Bifunctional enzyme Fae/Hps"
FT /id="PRO_0000236087"
FT REGION 1..164
FT /note="Formaldehyde-activating enzyme"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT REGION 165..406
FT /note="3-hexulose-6-phosphate synthase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
SQ SEQUENCE 406 AA; 44585 MW; 1AC3A236F144B49F CRC64;
MSDIYEIGEA LIGDGPELAH IDLIVGSKQG PVGTAFATNM ASMSVGHTPL LSVIRPNLPT
KPATLIVPKV TVQNLDDASK IFGPAQTAVG RAVADAVEEE IIPKDIVEDI VLMVNVFIDP
SAKDYRKIYQ YNYGATKLAI KRAFDKYPSV DKVLAEKDRG THPIMGFKAM KLWNPPYLQV
ALDLDNEDRM RSIIRDLPKR ERILIEAGTP LVKKFGVEII SKIREERPGA FIIADLKTLD
VGRVEVKMAA DETADAVAIS GLGTNESIEK AIHECSKQGI YSILDMMNVS DIPSKLEELK
LKPNIVLLHR NIDSETMRDN DGEQQSEWGN IKDIKSKLGK RGLIAVAGGV TPEKVDTALA
NGANIIIAGR YIIGSSDVRR AAEDFLRYLP QDSDTMRLAL DEDEKI
