G6PI_VIBCH
ID G6PI_VIBCH Reviewed; 550 AA.
AC Q9KUY4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
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};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
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}; OrderedLocusNames=VC_0374;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 -!- 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; AE003852; AAF93547.1; -; Genomic_DNA.
DR PIR; B82330; B82330.
DR RefSeq; NP_230028.1; NC_002505.1.
DR RefSeq; WP_000916643.1; NZ_LT906614.1.
DR PDB; 3HJB; X-ray; 1.50 A; A/B/C/D=1-550.
DR PDBsum; 3HJB; -.
DR AlphaFoldDB; Q9KUY4; -.
DR SMR; Q9KUY4; -.
DR STRING; 243277.VC_0374; -.
DR DNASU; 2615017; -.
DR EnsemblBacteria; AAF93547; AAF93547; VC_0374.
DR GeneID; 57739110; -.
DR KEGG; vch:VC_0374; -.
DR PATRIC; fig|243277.26.peg.350; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR BioCyc; VCHO:VC0374-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q9KUY4; -.
DR Proteomes; UP000000584; Chromosome 1.
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 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; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT CHAIN 1..550
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180762"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 387
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 515
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3HJB"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:3HJB"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3HJB"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3HJB"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 417..434
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 438..447
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 452..462
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 480..500
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:3HJB"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:3HJB"
FT HELIX 536..549
FT /evidence="ECO:0007829|PDB:3HJB"
SQ SEQUENCE 550 AA; 60691 MW; 5E38B0421C3A1B16 CRC64;
MLKNINPTQT QAWKALTAHF ESAQDMDLKA LFAQDSERFA KYSARFGQDI LVDYSKNLVN
AETMQHLFAL AKETDLQSAI TAMFKGEAIN QTEDRAVLHT ALRNRSNSPV LVNGEDVMPA
VNAVLAKMKA FSERVIGGEW KGFTGKAITD VVNIGIGGSD LGPYMVTEAL VPYKNHLTMH
FVSNVDGTHM AETLKNVDPE TTLFLVASKT FTTQETMTNA HTARDWFLKA AGDEAHVAKH
FAALSTNGKA VAEFGIDTDN MFEFWDWVGG RYSLWSAIGL SIILSIGYDN FVELLAGAHE
MDQHFVNTPF ESNIPVILAL IGIWYNNFHG AESEAILPYD QYLHRFAAYF QQGNMESNGK
YVDRNGNPVT YQTGPIIWGE PGTNGQHAFY QLIHQGTKLI PCDFIAPAVS HNLVGDHHQK
LMSNFFAQTE ALAFGKSAQA VQAELEKAGK SAAEIAALVP FKVFEGNRPT NSILVKQITP
RTLGNLIAMY EHKIFVQGVI WNIFSFDQWG VELGKQLANQ ILPELADSAA VTSHDSSTNG
LINAFKAFRA
