G6PI_CAUVC
ID G6PI_CAUVC Reviewed; 539 AA.
AC Q9ABK5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CC_0222;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK22209.1; -; Genomic_DNA.
DR PIR; E87276; E87276.
DR RefSeq; NP_419041.1; NC_002696.2.
DR RefSeq; WP_010918111.1; NC_002696.2.
DR AlphaFoldDB; Q9ABK5; -.
DR SMR; Q9ABK5; -.
DR STRING; 190650.CC_0222; -.
DR EnsemblBacteria; AAK22209; AAK22209; CC_0222.
DR KEGG; ccr:CC_0222; -.
DR PATRIC; fig|190650.5.peg.218; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OMA; IGVWYIN; -.
DR BioCyc; CAULO:CC0222-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001816; Chromosome.
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 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 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..539
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180617"
FT REGION 519..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 380
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 508
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 539 AA; 57526 MW; B233DFBAF7FD1595 CRC64;
MADLDAAWTR LEAAAKAAGD KRIVEFFDAE PGRLDALTLD VAGLHLDLSK QAWDEAGLEA
ALDLAHAADV EGARARMFDG EAINSSEGRA VLHTALRAPA GADVKALGQP VMAEVDAVRQ
RMKAFAQAVR SGAIKGATGK PFKAILHIGI GGSDLGPRLL WDALRPVKPS IDLRFVANVD
GAEFALTTAD MDPEETLVMV VSKTFTTQET MANAGAARAW LVAALGEQGA NQHLAAISTA
LDKTAAFGVP DDRVFGFWDW VGGRYSLWSS VSLSVAVAAG WDAFQGFLDG GAAMDEHFRT
APLEQNAPVL VALAQIFNRN GLDRRARSVV PYSHRLRRLA AFLQQLEMES NGKSVGPDGQ
PAKRGTATVV FGDEGTNVQH AYFQCMHQGT DITPMELIGV AKSDEGPAGM HEKLLSNLLA
QAEAFMVGRT TDDVVAELTA KGVSDAEIAT LAPQRTFAGN RPSTLVLLDR LTPQTFGALI
ALYEHKTFVE GVIWGINSFD QWGVELGKVM ANRILPELES GASGQHDPST AGLIQRLKR
