(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9B6_METMS

ID   D5E9B6_METMS            Unreviewed;       392 AA.
AC   D5E9B6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 57.
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   OrderedLocusNames=Mmah_0234 {ECO:0000313|EMBL:ADE35767.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35767.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35767.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; CP001994; ADE35767.1; -; Genomic_DNA.
DR   RefSeq; WP_013036710.1; NC_014002.1.
DR   EnsemblBacteria; ADE35767; ADE35767; Mmah_0234.
DR   GeneID; 8982366; -.
DR   KEGG; mmh:Mmah_0234; -.
DR   eggNOG; arCOG00053; Archaea.
DR   eggNOG; arCOG00103; Archaea.
DR   eggNOG; COG0269; LUCA.
DR   eggNOG; COG1795; LUCA.
DR   HOGENOM; HOG000286408; -.
DR   KO; K13812; -.
DR   OMA; YNYGATK; -.
DR   OrthoDB; 24053at2157; -.
DR   BioCyc; MMAH547558:G1GHT-232-MONOMER; -.
DR   UniPathway; UPA00293; -.
DR   Proteomes; UP000001059; 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;
DR   PRODOM; D5E9B6.
DR   SWISS-2DPAGE; D5E9B6.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01268};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01268, ECO:0000313|EMBL:ADE35767.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          174..374
FT                   /note="OMPdecase"
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                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         48
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         66
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         68
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         83
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
SQ   SEQUENCE   392 AA;  42423 MW;  79EE87DE13B7B48B CRC64;
     MMLIGEALIG EEPELAHIDL MIGDKEGPVG QAFATGMTQL SAGHTPLLSV IRPNLPTKPS
     TLIVPKVTVK NMDQASQIFG PAQAAVSKAV ADAVEEGIVP KEKADDLVIV ASVFIHPQAL
     DYNRIYRYNY GATKLALKRA MENFPAVDTV LDEKDKGSHA VMGFKVSRLW DPPYLQVALD
     NPNLEAVLNV VRQLPKSDHL ILEAGTPLIK RYGVDVITKL REVKPDAFIV ADLKTLDTGN
     LEARMVADAT ADAIVVSALA PIPTLEKAIS EAHKTGIYAV MDTLNQPDPM AVLKELNELP
     DVVELHRAID VEDTAYAWGS IDAIKELSPK ILVAVAGGVR VHTIPDALKA GADILVVGRA
     ITNSKDIRQS AEQFVEGLNK PEIDQFRVMT DF
//

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