ID A0A166AG45_9EURY Unreviewed; 407 AA.
AC A0A166AG45;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Bifunctional enzyme Fae/Hps {ECO:0000256|HAMAP-Rule:MF_01268};
DE Includes:
DE RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase {ECO:0000256|HAMAP-Rule:MF_01268};
DE EC=4.2.1.147 {ECO:0000256|HAMAP-Rule:MF_01268};
DE AltName: Full=Formaldehyde-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01268};
DE Short=Fae {ECO:0000256|HAMAP-Rule:MF_01268};
DE Includes:
DE RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01268};
DE Short=HPS {ECO:0000256|HAMAP-Rule:MF_01268};
DE EC=4.1.2.43 {ECO:0000256|HAMAP-Rule:MF_01268};
DE AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase {ECO:0000256|HAMAP-Rule:MF_01268};
GN Name=fae {ECO:0000313|EMBL:KZX11989.1};
GN Synonyms=fae-hps {ECO:0000256|HAMAP-Rule:MF_01268};
GN ORFNames=MBFIL_12690 {ECO:0000313|EMBL:KZX11989.1};
OS Methanobrevibacter filiformis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=55758 {ECO:0000313|EMBL:KZX11989.1, ECO:0000313|Proteomes:UP000077066};
RN [1] {ECO:0000313|EMBL:KZX11989.1, ECO:0000313|Proteomes:UP000077066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11501 {ECO:0000313|EMBL:KZX11989.1,
RC ECO:0000313|Proteomes:UP000077066};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter filiformis DSM 11501.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC tetrahydromethanopterin (H(4)MPT) to 5,10-
CC methylenetetrahydromethanopterin. {ECO:0000256|HAMAP-Rule:MF_01268}.
CC -!- FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate
CC and formaldehyde from 3-hexulose-6-phosphate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01268};
CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01268}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family.
CC HPS subfamily. {ECO:0000256|HAMAP-Rule:MF_01268}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the formaldehyde-
CC activating enzyme family. {ECO:0000256|HAMAP-Rule:MF_01268}.
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:KZX11989.1}.
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DR EMBL; LWMT01000238; KZX11989.1; -; Genomic_DNA.
DR RefSeq; WP_066972809.1; NZ_LWMT01000238.1.
DR AlphaFoldDB; A0A166AG45; -.
DR STRING; 55758.MBFIL_12690; -.
DR PATRIC; fig|55758.3.peg.1449; -.
DR OrthoDB; 64276at2157; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000077066; Unassembled WGS sequence.
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; Aldolase class I; 1.
DR Gene3D; 3.30.230.60; Formaldehyde-activating enzyme; 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_Su5_D2-typ_SF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR03126; one_C_fae; 1.
DR PANTHER; PTHR35039; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR PANTHER; PTHR35039:SF3; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR Pfam; PF08714; Fae; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01268};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01268};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01268};
KW Reference proteome {ECO:0000313|Proteomes:UP000077066}.
FT DOMAIN 174..386
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT REGION 1..161
FT /note="Formaldehyde-activating enzyme"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT REGION 162..407
FT /note="3-hexulose-6-phosphate synthase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT ACT_SITE 17
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
SQ SEQUENCE 407 AA; 44595 MW; 9BEF7C96D35D3224 CRC64;
MYEIGEALIG DGNELAHVDL IIGTKDSPAG TAFANGMSQL SIGHTPVLSV IRPNLMTKPA
TLIVPKVTVG NLDDASKIFG PAQTAVGRAV ADAVDEGIIP KKDIEDLVII ASVFIHPEAK
DYRKIYQYNY GATKLAIKRA LKKYPSIKKV LAEKDRGTHP IMGFRVTKLW KPPYLQVALD
LDNVDVMERI IEATPDRERI LLEAGTPLIK KFGVGIVSKI RELRPDAFII ADLKTLDVGR
IEVKMAADET ADAVAISGLG TLESIEKAIH ETQRQGIYSI LDMMNVKNFE EKLREINPEL
KPNIVLLHRN VDSETSKTEK GESTANMTDW GNIKAIKEIL GKGLVAVAGG ITPSNMEEAL
DSEADIIIAG RYITSSRNVT RAVEDFLAHM PQDPDNMRLP LDEDESV
//
