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HPS_MYCGS
ID   HPS_MYCGS               Reviewed;         207 AA.
AC   Q9LBW4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=3-hexulose-6-phosphate synthase;
DE            Short=HPS;
DE            EC=4.1.2.43;
DE   AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase;
GN   Name=rmpA;
OS   Mycobacterium gastri.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TRANSCRIPTIONAL
RP   REGULATION.
RC   STRAIN=MB19;
RX   PubMed=10648518; DOI=10.1128/jb.182.4.944-948.2000;
RA   Mitsui R., Sakai Y., Yasueda H., Kato N.;
RT   "A novel operon encoding formaldehyde fixation: the ribulose monophosphate
RT   pathway in the Gram-positive facultative methylotrophic bacterium
RT   Mycobacterium gastri MB19.";
RL   J. Bacteriol. 182:944-948(2000).
CC   -!- FUNCTION: Catalyzes the condensation of ribulose 5-phosphate with
CC       formaldehyde to form 3-hexulose 6-phosphate.
CC       {ECO:0000269|PubMed:10648518}.
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   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via RuMP
CC       pathway; D-fructose 6-phosphate from D-ribulose 5-phosphate and
CC       formaldehyde: step 1/2.
CC   -!- INDUCTION: By methanol or methylamine. {ECO:0000269|PubMed:10648518}.
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. HPS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB034913; BAA90546.1; -; Genomic_DNA.
DR   PDB; 3AJX; X-ray; 1.60 A; A/B/C/D=1-207.
DR   PDBsum; 3AJX; -.
DR   AlphaFoldDB; Q9LBW4; -.
DR   SMR; Q9LBW4; -.
DR   BRENDA; 4.1.2.43; 10297.
DR   UniPathway; UPA00294; UER00434.
DR   EvolutionaryTrace; Q9LBW4; -.
DR   GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-EC.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019647; P:formaldehyde assimilation via ribulose monophosphate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04726; KGPDC_HPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR017553; 3-hexulose-6-phosphate_synth.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041710; HPS/KGPDC.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR03128; RuMP_HxlA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Lyase; One-carbon metabolism.
FT   CHAIN           1..207
FT                   /note="3-hexulose-6-phosphate synthase"
FT                   /id="PRO_0000235167"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           33..39
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           42..50
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          54..62
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           66..75
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           89..102
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           137..140
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           148..157
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           172..177
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           187..190
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:3AJX"
FT   HELIX           195..204
FT                   /evidence="ECO:0007829|PDB:3AJX"
SQ   SEQUENCE   207 AA;  20936 MW;  50A77E4688F937D2 CRC64;
     MKLQVAIDLL STEAALELAG KVAEYVDIIE LGTPLIEAEG LSVITAVKKA HPDKIVFADM
     KTMDAGELEA DIAFKAGADL VTVLGSADDS TIAGAVKAAQ AHNKGVVVDL IGIEDKATRA
     QEVRALGAKF VEMHAGLDEQ AKPGFDLNGL LAAGEKARVP FSVAGGVKVA TIPAVQKAGA
     EVAVAGGAIY GAADPAAAAK ELRAAIA
 
 
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