G6PI_THEMA
ID G6PI_THEMA Reviewed; 448 AA.
AC Q9X1A5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000269|PubMed:33422670};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000303|PubMed:33422670};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000303|PubMed:33422670};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=TmPGI {ECO:0000303|PubMed:33422670};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=TM_1385;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP GLU-281; HIS-310; GLN-415 AND LYS-422.
RX PubMed=33422670; DOI=10.1016/j.bbapap.2021.140602;
RA Swope N., Lake K.E., Barrow G.H., Yu D., Fox D.A., Columbus L.;
RT "TM1385 from Thermotoga maritima functions as a phosphoglucose isomerase
RT via cis-enediol-based mechanism with active site redundancy.";
RL Biochim. Biophys. Acta 1869:140602-140602(2021).
RN [3] {ECO:0007744|PDB:2Q8N}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of glucose-6-phosphate isomerase (EC 5.3.1.9) (TM1385)
RT from Thermotoga maritima at 1.82 A resolution.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. Does not have phosphomannose isomerase (PMI)
CC activity. Isomerization proceeds through a cis-enediol-based mechanism.
CC {ECO:0000269|PubMed:33422670}.
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 ECO:0000269|PubMed:33422670};
CC -!- ACTIVITY REGULATION: Optimal activity is achieved when His-310 and Lys-
CC 422 are both present to open the sugar ring, and Glu-281 catalyzes the
CC isomerization step (PubMed:33422670). Activity is decreased in the
CC presence of the PGI inhibitor 6-phosphogluconate (PubMed:33422670).
CC {ECO:0000269|PubMed:33422670}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for fructose 6-phosphate {ECO:0000269|PubMed:33422670};
CC Note=kcat is 17.4 sec(-1) with fructose 6-phosphate as substrate.
CC {ECO:0000269|PubMed:33422670};
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. {ECO:0000305|PubMed:33422670}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; AE000512; AAD36455.1; -; Genomic_DNA.
DR PIR; B72262; B72262.
DR RefSeq; NP_229186.1; NC_000853.1.
DR RefSeq; WP_004081585.1; NZ_CP011107.1.
DR PDB; 2Q8N; X-ray; 1.82 A; A/B/C=1-448.
DR PDBsum; 2Q8N; -.
DR AlphaFoldDB; Q9X1A5; -.
DR SMR; Q9X1A5; -.
DR STRING; 243274.THEMA_07400; -.
DR EnsemblBacteria; AAD36455; AAD36455; TM_1385.
DR KEGG; tma:TM1385; -.
DR eggNOG; COG0166; Bacteria.
DR InParanoid; Q9X1A5; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
DR BioCyc; MetaCyc:MON-381; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q9X1A5; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; 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;
KW Reference proteome.
FT CHAIN 1..448
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180757"
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000305|PubMed:33422670"
FT ACT_SITE 310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000305|PubMed:33422670"
FT ACT_SITE 422
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000305|PubMed:33422670"
FT MUTAGEN 281
FT /note="E->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:33422670"
FT MUTAGEN 310
FT /note="H->A: 200-fold decrease in catalytic efficiency.
FT Loss of activity; when associated with A-422."
FT /evidence="ECO:0000269|PubMed:33422670"
FT MUTAGEN 415
FT /note="Q->A: 300-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:33422670"
FT MUTAGEN 422
FT /note="K->A: 300-fold decrease in catalytic efficiency.
FT Loss of activity; when associated with A-310."
FT /evidence="ECO:0000269|PubMed:33422670"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2Q8N"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2Q8N"
FT TURN 98..103
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2Q8N"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2Q8N"
FT TURN 348..352
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 355..372
FT /evidence="ECO:0007829|PDB:2Q8N"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 387..407
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:2Q8N"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:2Q8N"
SQ SEQUENCE 448 AA; 50493 MW; 7FDE91F297851F71 CRC64;
MSLKFDFSNL FEPNISGGLT DEDVKSVEEK VTSAVRNFVE NTPDFAKLDR SWIDSVKSLE
DWIINFDTVV VLGIGGSGLG NLALHYSLRP LNWNEMTREE RNGYARVFVV DNVDPDLMSS
VLDRIDPKTT LFNVISKSGS TAEVMATYSI ARGILEAYGL DPREHMLITT DPEKGFLRKL
VKEEGFRSLE VPPGVGGRFS VLTPVGLLSA MAEGIDIDEL HEGAKDAFEK SMKENILENP
AAMIALTHYL YLNKGKSISV MMAYSNRMIY LVDWYRQLWA ESLGKRYNLK GEEVFTGQTP
VKALGATDQH SQIQLYNEGP NDKVITFLRV ENFDREIVIP ETGRAELSYL ARKKLSELLL
AEQTGTEEAL RENNRPNMRV TFDGLTPYNV GQFFAYYEAA TAFMGYLLEI NPFDQPGVEL
GKKITFALMG REGYTYEIKE RSKKVIIE
