ID A0A166CLI6_9EURY Unreviewed; 408 AA.
AC A0A166CLI6;
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:KZX14635.1};
GN Synonyms=fae-hps {ECO:0000256|HAMAP-Rule:MF_01268};
GN ORFNames=MBCUT_20250 {ECO:0000313|EMBL:KZX14635.1};
OS Methanobrevibacter cuticularis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX14635.1, ECO:0000313|Proteomes:UP000077275};
RN [1] {ECO:0000313|EMBL:KZX14635.1, ECO:0000313|Proteomes:UP000077275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX14635.1,
RC ECO:0000313|Proteomes:UP000077275};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
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:KZX14635.1}.
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DR EMBL; LWMW01000158; KZX14635.1; -; Genomic_DNA.
DR RefSeq; WP_067260650.1; NZ_LWMW01000158.1.
DR AlphaFoldDB; A0A166CLI6; -.
DR STRING; 47311.MBCUT_20250; -.
DR PATRIC; fig|47311.3.peg.2211; -.
DR OrthoDB; 64276at2157; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000077275; 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:UP000077275}.
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..408
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 408 AA; 44372 MW; A1B26D8C1B2166F4 CRC64;
MYKIGEALIG DGNELAHIDL IIGDKESAAG SAFANGMSQL SIGHTPLLSV IRPNLMTKPA
TLIVPKVTVG DLDDASKIFG PAQTAVGRAV ADAVEEGLIP KDQSEDLVII ISVFIHPEAK
DYRKIYQYNY GATKLAIRRA MGDYPSIDKV LAEKDRGTHP IMGFKVTRLW SPPYLQVALD
LDNLDTMEKI IAAIPDRERV LLEAGTPLIK KFGVGVVNKI RELRPDAFII ADLKTLDVGR
VEVKMAADET ADAIAISGLG TIESIEKAIH EAQKQGIYSI LDMMNVSNFT DKLNQINENL
KPDIVLLHRN VDLETSKAEK GEDTSSMTEW GNIKEIKNLI GNGLVAVAGG ITPAKVEEAI
DSGADIIVVG RYIIGSRDVR RSAEDFLSHL PQDPDNMRLA LDEDESAN
//
