G6PI2_GEOSE
ID G6PI2_GEOSE Reviewed; 445 AA.
AC P13376;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glucose-6-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi2 {ECO:0000255|HAMAP-Rule:MF_00473}; Synonyms=pgiB;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T521;
RX PubMed=2532320; DOI=10.1093/nar/17.23.10107;
RA Tao W., Wang L., Shen R., Sheng Z.;
RT "Complete nucleotide sequences of two phosphoglucoisomerase isozymes from
RT Bacillus stearothermophilus.";
RL Nucleic Acids Res. 17:10107-10108(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10318897; DOI=10.1073/pnas.96.10.5412;
RA Sun Y.-J., Chou C.-C., Chen W.-S., Wu R.-T., Meng M., Hsiao C.-D.;
RT "The crystal structure of a multifunctional protein: phosphoglucose
RT isomerase/autocrine motility factor/neuroleukin.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5412-5417(1999).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473, ECO:0000305}.
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DR EMBL; X16640; CAA34635.1; -; Genomic_DNA.
DR PIR; S06198; NUBSS.
DR PDB; 1B0Z; X-ray; 2.30 A; A=1-445.
DR PDB; 1C7Q; X-ray; 2.30 A; A=1-445.
DR PDB; 1C7R; X-ray; 2.50 A; A=1-445.
DR PDB; 2PGI; X-ray; 2.30 A; A=1-445.
DR PDBsum; 1B0Z; -.
DR PDBsum; 1C7Q; -.
DR PDBsum; 1C7R; -.
DR PDBsum; 2PGI; -.
DR AlphaFoldDB; P13376; -.
DR SMR; P13376; -.
DR DrugBank; DB03042; 5-Phosphoarabinonic Acid.
DR DrugBank; DB02257; N-Bromoacetyl-Aminoethyl Phosphate.
DR BRENDA; 5.3.1.9; 623.
DR SABIO-RK; P13376; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P13376; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..445
FT /note="Glucose-6-phosphate isomerase 2"
FT /id="PRO_0000180592"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 306
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 420
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1B0Z"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1C7Q"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1B0Z"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1C7Q"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1B0Z"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:1B0Z"
FT TURN 346..350
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:1B0Z"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 385..406
FT /evidence="ECO:0007829|PDB:1B0Z"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:1B0Z"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:1C7Q"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:1B0Z"
SQ SEQUENCE 445 AA; 50141 MW; 078AD337669D1AE1 CRC64;
MAISFDYSNA LPFMQENELD YLSEFVKAAH HMLHERKGPG SDFLGWVDWP IRYDKNEFSR
IKQAAERIRN HSDALVVIGI GGSYLGARAA IEALSHTFHN QMNDTTQIYF AGQNISSTYI
SHLLDVLEGK DLSINVISKS GTTTEPAIAF RIFRDYMEKK YGKEEARKRI YVTTDRTKGA
LKKLADQEGY ETFVIPDNIG GRYSVLTAVG LLPIAVAGLN IDRMMEGAAS AYHKYNNPDL
LTNESYQYAA VRNILYRKGK AIELLVNYEP SLHYVSEWWK QLFGESEGKD QKGLFPASVD
FTTDLHSMGQ YVQEGRRNLI ETVLHVKKPQ IELTIQEDPE NIDGLNFLAG KTLDEVNKKA
FQGTLLAHVD GGVPNLIVEL DEMNEYTFGE MVYFFEKACG ISGHLLGVNP FDQPGVEAYK
KNMFALLGKP GFEDEKAALM KRLSK
