PHI_METJA
ID PHI_METJA Reviewed; 180 AA.
AC Q58644;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=phi; OrderedLocusNames=MJ1247;
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 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CITRIC ACID,
RP FUNCTION, AND SUBUNIT.
RX PubMed=11839305; DOI=10.1016/s0969-2126(02)00701-3;
RA Martinez-Cruz L.A., Dreyer M.K., Boisvert D.C., Yokota H.,
RA Martinez-Chantar M.L., Kim R., Kim S.-H.;
RT "Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution
RT infers a molecular function of 3-hexulose-6-phosphate isomerase.";
RL Structure 10:195-204(2002).
CC -!- FUNCTION: Catalyzes the isomerization between 3-hexulose 6-phosphate
CC and fructose 6-phosphate. {ECO:0000269|PubMed:11839305}.
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: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC {ECO:0000269|PubMed:16237021}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11839305}.
CC -!- SIMILARITY: Belongs to the SIS family. PHI subfamily. {ECO:0000305}.
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DR EMBL; L77117; AAB99251.1; -; Genomic_DNA.
DR PIR; F64455; F64455.
DR PDB; 1JEO; X-ray; 2.00 A; A=1-180.
DR PDBsum; 1JEO; -.
DR AlphaFoldDB; Q58644; -.
DR SMR; Q58644; -.
DR STRING; 243232.MJ_1247; -.
DR EnsemblBacteria; AAB99251; AAB99251; MJ_1247.
DR KEGG; mja:MJ_1247; -.
DR eggNOG; arCOG00068; Archaea.
DR HOGENOM; CLU_094236_1_1_2; -.
DR InParanoid; Q58644; -.
DR OMA; KTIQPMG; -.
DR PhylomeDB; Q58644; -.
DR BRENDA; 5.3.1.27; 3260.
DR UniPathway; UPA00293; -.
DR EvolutionaryTrace; Q58644; -.
DR Proteomes; UP000000805; Chromosome.
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 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..180
FT /note="3-hexulose-6-phosphate isomerase"
FT /id="PRO_0000136568"
FT DOMAIN 33..167
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 90..95
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:1JEO"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 49..64
FT /evidence="ECO:0007829|PDB:1JEO"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1JEO"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:1JEO"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1JEO"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 144..164
FT /evidence="ECO:0007829|PDB:1JEO"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:1JEO"
SQ SEQUENCE 180 AA; 20443 MW; 7C3D607BCBD4AA0A CRC64;
MSKLEELDIV SNNILILKKF YTNDEWKNKL DSLIDRIIKA KKIFIFGVGR SGYIGRCFAM
RLMHLGFKSY FVGETTTPSY EKDDLLILIS GSGRTESVLT VAKKAKNINN NIIAIVCECG
NVVEFADLTI PLEVKKSKYL PMGTTFEETA LIFLDLVIAE IMKRLNLDES EIIKRHCNLL
