PHI_MYCGS
ID PHI_MYCGS Reviewed; 199 AA.
AC Q9LBW5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 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 isomerization between 3-hexulose 6-phosphate
CC and fructose 6-phosphate. {ECO:0000269|PubMed:10648518}.
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 -!- INDUCTION: By methanol or methylamine. {ECO:0000269|PubMed:10648518}.
CC -!- SIMILARITY: Belongs to the SIS family. PHI subfamily. {ECO:0000305}.
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DR EMBL; AB034913; BAA90545.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LBW5; -.
DR SMR; Q9LBW5; -.
DR BRENDA; 5.3.1.27; 10297.
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 TIGRFAMs; TIGR03127; RuMP_HxlB; 1.
DR PROSITE; PS51464; SIS; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Isomerase.
FT CHAIN 1..199
FT /note="3-hexulose-6-phosphate isomerase"
FT /id="PRO_0000235171"
FT DOMAIN 44..186
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 101..106
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 199 AA; 20770 MW; EBFEAADABBB2D786 CRC64;
MTQAAEADGA VKVVGDDITN NLSLVRDEVA DTAAKVDPEQ VAVLARQIVQ PGRVFVAGAG
RSGLVLRMAA MRLMHFGLTV HVAGDTTTPA ISAGDLLLVA SGSGTTSGVV KSAETAKKAG
ARIAAFTTNP DSPLAGLADA VVIIPAAQKT DHGSHISRQY AGSLFEQVLF VVTEAVFQSL
WDHTEVEAEE LWTRHANLE