FAEHP_METJA
ID FAEHP_METJA Reviewed; 381 AA.
AC Q58842;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 105.
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, ECO:0000303|PubMed:16237021};
DE Short=Fae {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021};
DE Includes:
DE RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021};
DE Short=HPS {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021};
DE EC=4.1.2.43 {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16237021};
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=MJ1447;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A HPS, AND PATHWAY.
RX PubMed=16237021; DOI=10.1128/jb.187.21.7382-7389.2005;
RA Grochowski L.L., Xu H., White R.H.;
RT "Ribose-5-phosphate biosynthesis in Methanocaldococcus jannaschii occurs in
RT the absence of a pentose-phosphate pathway.";
RL J. Bacteriol. 187:7382-7389(2005).
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 ECO:0000303|PubMed:16237021}.
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, ECO:0000269|PubMed:16237021}.
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 ECO:0000269|PubMed:16237021};
CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16237021}.
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}.
CC -!- CAUTION: Ile-16 is present instead of the conserved His which is
CC expected to be an active site residue. Substrate-binding sites are also
CC not conserved. Thus, this enzyme may not display fae activity.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99456.1; -; Genomic_DNA.
DR PIR; F64480; F64480.
DR RefSeq; WP_010870967.1; NC_000909.1.
DR AlphaFoldDB; Q58842; -.
DR SMR; Q58842; -.
DR STRING; 243232.MJ_1447; -.
DR DNASU; 1452351; -.
DR EnsemblBacteria; AAB99456; AAB99456; MJ_1447.
DR GeneID; 1452351; -.
DR KEGG; mja:MJ_1447; -.
DR eggNOG; arCOG00103; Archaea.
DR HOGENOM; CLU_701335_0_0_2; -.
DR InParanoid; Q58842; -.
DR OMA; LWDPPYL; -.
DR OrthoDB; 24053at2157; -.
DR PhylomeDB; Q58842; -.
DR UniPathway; UPA00293; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IBA:GO_Central.
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 GO; GO:0019854; P:L-ascorbic acid catabolic process; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Multifunctional enzyme; Reference proteome.
FT CHAIN 1..381
FT /note="Bifunctional enzyme Fae/Hps"
FT /id="PRO_0000212107"
FT REGION 1..150
FT /note="Formaldehyde-activating enzyme"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT REGION 151..381
FT /note="3-hexulose-6-phosphate synthase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
SQ SEQUENCE 381 AA; 42990 MW; BB4C460AE796FAA3 CRC64;
MIKFGEAVLG NEIKAIVNVA LGKGELIENT FTNALTRGNC VFANLRPNLI VKPLTLVVPR
HNIESEIQDE LFQGVIQYAV AKAVADLDLD EDLKVVVSVN VPEVPITNLN KRKLFQYFYA
SAKLAINRAL NEYPSKEKVK KEKYRALHPL VGFRDVRLEY PPYLQIALDV PTMENLEFLL
QTIPNSDHII LEAGTPLIKK FGLEVIEIMR EYFDGFIVAD LKTLDTGRVE VRLAFEATAN
AVAISGVAPK STIIKAIHEC QKCGLISYLD MMNVSEPQKL YDSLKLKPDV VILHRGIDEE
TFGIKKEWKF KENCLLAIAG GVGVENVEEL LKEYQILIVG RAITKSKDPG RVIRMFINKM
GYDIDTYRLY FDEDEDIGEE L
