PHI_METAM
ID PHI_METAM Reviewed; 181 AA.
AC Q9S0X3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=3-hexulose-6-phosphate isomerase;
DE EC=5.3.1.27;
DE AltName: Full=6-phospho-3-hexuloisomerase;
DE Short=PHI;
GN Name=rmpB;
OS Methylomonas aminofaciens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=46896;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=77a;
RX PubMed=10418139; DOI=10.1111/j.1574-6968.1999.tb13652.x;
RA Sakai Y., Mitsui R., Katayama Y., Yanase H., Kato N.;
RT "Organization of the genes involved in the ribulose monophosphate pathway
RT in an obligate methylotrophic bacterium, Methylomonas aminofaciens 77a.";
RL FEMS Microbiol. Lett. 176:125-130(1999).
CC -!- FUNCTION: Catalyzes the isomerization between 3-hexulose 6-phosphate
CC and fructose 6-phosphate. {ECO:0000269|PubMed:10418139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabino-hex-3-ulose 6-phosphate = beta-D-fructose 6-
CC phosphate; Xref=Rhea:RHEA:25900, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:58542; EC=5.3.1.27;
CC -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via RuMP
CC pathway; D-fructose 6-phosphate from D-ribulose 5-phosphate and
CC formaldehyde: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10418139}.
CC -!- SIMILARITY: Belongs to the SIS family. PHI subfamily. {ECO:0000305}.
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DR EMBL; AB026428; BAA83098.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S0X3; -.
DR SMR; Q9S0X3; -.
DR BRENDA; 5.3.1.27; 7933.
DR UniPathway; UPA00294; UER00435.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0043800; F:hexulose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic 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 CDD; cd05005; SIS_PHI; 1.
DR InterPro; IPR017552; PHI/rmpB.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR43443; PTHR43443; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Isomerase.
FT CHAIN 1..181
FT /note="3-hexulose-6-phosphate isomerase"
FT /id="PRO_0000136567"
FT DOMAIN 27..168
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 84..89
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 181 AA; 19345 MW; FE9AE4FDFAB13AB7 CRC64;
MNKYQELVVS KLTNVINNTA EGYDDKILSL VDAAGRTFIG GAGRSLLVSR FFAMRLVHAG
YQVSMVGEVV TPSIQAGDLF IVISGSGSTE TLMPLVKKAK SQGAKIIVIS MKAQSPMAEL
ADLVVPVGGN DANAFDKTHG MPMGTIFELS TLWFLEATIA KLVDQKGLTE EGMRAIHANL
E