ID W9DPR6_METTI Unreviewed; 392 AA.
AC W9DPR6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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-hps {ECO:0000256|HAMAP-Rule:MF_01268};
GN ORFNames=MettiDRAFT_1836 {ECO:0000313|EMBL:ETA68369.1};
OS Methanolobus tindarius DSM 2278.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=1090322 {ECO:0000313|EMBL:ETA68369.1, ECO:0000313|Proteomes:UP000019483};
RN [1] {ECO:0000313|EMBL:ETA68369.1, ECO:0000313|Proteomes:UP000019483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2278 {ECO:0000313|EMBL:ETA68369.1,
RC ECO:0000313|Proteomes:UP000019483};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (AUG-2013) 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:ETA68369.1}.
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DR EMBL; AZAJ01000001; ETA68369.1; -; Genomic_DNA.
DR RefSeq; WP_023845504.1; NZ_AZAJ01000001.1.
DR AlphaFoldDB; W9DPR6; -.
DR STRING; 1090322.MettiDRAFT_1836; -.
DR OrthoDB; 64276at2157; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000019483; 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}.
FT DOMAIN 174..374
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..392
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 392 AA; 42324 MW; 6C3C84106D593ADB CRC64;
MLLIGEALIG EEPELAHVDL MIGNKDGPVG QAFANGLTQL SAGHTPLLSV VRPNLPTKPA
TLIVPKVTVK NMGQAAQIFG PAQAAVAKAV ADALEEGTFG DLDIEDLVVV ASVFIHPEAK
DYNRIYRYNY GATKLAVKRA VDGFPDIDTV LKEKDRMGHA IMGFKVSRLW NPPYLQVALD
NPNLPVIQNI VKQIPKSDHV ILEAGTPLIK RYGVDVITKL REIRPDAFIV ADLKTLDTGN
LEARMVADAT ADAIVVSALA PIATMNKAIE EAHKTGIYAI MDTLNCDDPV AVLKQLDVLP
DVVELHRGID IEETEHAWGN IDAIKALSPK ILVAVAGGVR INTMPQALKA GADVLVVGRA
ITNAKDVRQV AEKFIEGLNN PEIDQFRVMT DF
//