G6PI_MYCTU
ID G6PI_MYCTU Reviewed; 553 AA.
AC P9WN69; L0T6W0; P64192; P77895;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
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:16212940, ECO:0000269|PubMed:17126561, ECO:0000269|PubMed:20445242};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000303|PubMed:16212940};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000303|PubMed:16212940};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000303|PubMed:16212940};
GN OrderedLocusNames=Rv0946c; ORFNames=MTCY10D7.28;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=16212940; DOI=10.1016/j.bbrc.2005.09.092;
RA Mathur D., Ahsan Z., Tiwari M., Garg L.C.;
RT "Biochemical characterization of recombinant phosphoglucose isomerase of
RT Mycobacterium tuberculosis.";
RL Biochem. Biophys. Res. Commun. 337:626-632(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=H37Rv;
RX PubMed=17126561; DOI=10.1016/j.pep.2006.10.006;
RA Mathur D., Garg L.C.;
RT "Functional phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv:
RT rapid purification with high yield and purity.";
RL Protein Expr. Purif. 52:373-378(2007).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=17401215; DOI=10.1107/s1744309107013218;
RA Mathur D., Anand K., Mathur D., Jagadish N., Suri A., Garg L.C.;
RT "Crystallization and preliminary X-ray characterization of phosphoglucose
RT isomerase from Mycobacterium tuberculosis H37Rv.";
RL Acta Crystallogr. F 63:353-355(2007).
RN [6] {ECO:0007744|PDB:2WU8}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 7-553, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLY-158 AND THR-212.
RC STRAIN=H37Rv;
RX PubMed=20445242; DOI=10.1107/s1744309110011656;
RA Anand K., Mathur D., Anant A., Garg L.C.;
RT "Structural studies of phosphoglucose isomerase from Mycobacterium
RT tuberculosis H37Rv.";
RL Acta Crystallogr. F Struct. Biol. Commun. 66:490-497(2010).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473,
CC ECO:0000269|PubMed:16212940, ECO:0000269|PubMed:17126561,
CC ECO:0000269|PubMed:20445242}.
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:16212940, ECO:0000269|PubMed:17126561,
CC ECO:0000269|PubMed:20445242};
CC -!- ACTIVITY REGULATION: Activity is decreased in the presence of the PGI
CC inhibitor 6-phosphogluconate (PubMed:16212940, PubMed:17126561). Does
CC not require mono- or divalent cations for activity (PubMed:16212940,
CC PubMed:17126561). {ECO:0000269|PubMed:16212940,
CC ECO:0000269|PubMed:17126561}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.318 mM for fructose-6-phosphate {ECO:0000269|PubMed:16212940};
CC KM=0.27 mM for fructose-6-phosphate (for six-histidine-tag protein)
CC {ECO:0000269|PubMed:17126561};
CC Vmax=0.032 umol/min/mg enzyme with fructose-6-phosphate as substrate
CC {ECO:0000269|PubMed:16212940, ECO:0000269|PubMed:17126561};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:16212940,
CC ECO:0000269|PubMed:17126561};
CC Temperature dependence:
CC Optimum temperature is from 20 to 40 degrees Celsius. Retains full
CC activity up to 50 degrees Celsius (PubMed:16212940). Retains full
CC activity up to 45 degrees Celsius (for six-histidine-tag protein)
CC (PubMed:17126561). {ECO:0000269|PubMed:16212940,
CC ECO:0000269|PubMed:17126561};
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:0000269|PubMed:16212940,
CC ECO:0000269|PubMed:20445242}.
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; AL123456; CCP43694.1; -; Genomic_DNA.
DR PIR; H70715; H70715.
DR RefSeq; NP_215461.1; NC_000962.3.
DR RefSeq; WP_003404830.1; NZ_NVQJ01000001.1.
DR PDB; 2WU8; X-ray; 2.25 A; A=7-553.
DR PDBsum; 2WU8; -.
DR AlphaFoldDB; P9WN69; -.
DR SMR; P9WN69; -.
DR STRING; 83332.Rv0946c; -.
DR iPTMnet; P9WN69; -.
DR PaxDb; P9WN69; -.
DR DNASU; 885533; -.
DR GeneID; 45424915; -.
DR GeneID; 885533; -.
DR KEGG; mtu:Rv0946c; -.
DR TubercuList; Rv0946c; -.
DR eggNOG; COG0166; Bacteria.
DR OMA; IGVWYIN; -.
DR PhylomeDB; P9WN69; -.
DR BioCyc; MetaCyc:G185E-5101-MON; -.
DR BRENDA; 5.3.1.9; 3445.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:MTBBASE.
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; IDA:MTBBASE.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
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; Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis;
KW Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..553
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180677"
FT REGION 524..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 388
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 514
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MUTAGEN 158
FT /note="G->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20445242"
FT MUTAGEN 212
FT /note="T->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:20445242"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2WU8"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 118..138
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:2WU8"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2WU8"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 289..308
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 315..329
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2WU8"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 424..441
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:2WU8"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 479..500
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 511..525
FT /evidence="ECO:0007829|PDB:2WU8"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2WU8"
FT HELIX 536..548
FT /evidence="ECO:0007829|PDB:2WU8"
SQ SEQUENCE 553 AA; 59974 MW; FB57DFFD16386AE4 CRC64;
MTSAPIPDIT ATPAWDALRR HHDQIGNTHL RQFFADDPGR GRELTVSVGD LYIDYSKHRV
TRETLALLID LARTAHLEER RDQMFAGVHI NTSEDRAVLH TALRLPRDAE LVVDGQDVVT
DVHAVLDAMG AFTDRLRSGE WTGATGKRIS TVVNIGIGGS DLGPVMVYQA LRHYADAGIS
ARFVSNVDPA DLIATLADLD PATTLFIVAS KTFSTLETLT NATAARRWLT DALGDAAVSR
HFVAVSTNKR LVDDFGINTD NMFGFWDWVG GRYSVDSAIG LSLMTVIGRD AFADFLAGFH
IIDRHFATAP LESNAPVLLG LIGLWYSNFF GAQSRTVLPY SNDLSRFPAY LQQLTMESNG
KSTRADGSPV SADTGEIFWG EPGTNGQHAF YQLLHQGTRL VPADFIGFAQ PLDDLPTAEG
TGSMHDLLMS NFFAQTQVLA FGKTAEEIAA DGTPAHVVAH KVMPGNRPST SILASRLTPS
VLGQLIALYE HQVFTEGVVW GIDSFDQWGV ELGKTQAKAL LPVITGAGSP PPQSDSSTDG
LVRRYRTERG RAG
