ID B4W5J4_9CAUL Unreviewed; 353 AA.
AC B4W5J4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN ORFNames=BBAL3_3177 {ECO:0000313|EMBL:EDX82020.1};
OS Brevundimonas sp. BAL3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=391600 {ECO:0000313|EMBL:EDX82020.1, ECO:0000313|Proteomes:UP000003957};
RN [1] {ECO:0000313|EMBL:EDX82020.1, ECO:0000313|Proteomes:UP000003957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL3 {ECO:0000313|EMBL:EDX82020.1,
RC ECO:0000313|Proteomes:UP000003957};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00473,
CC ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|HAMAP-
CC Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
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DR EMBL; DS989898; EDX82020.1; -; Genomic_DNA.
DR AlphaFoldDB; B4W5J4; -.
DR HOGENOM; CLU_017947_0_0_5; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000003957; Unassembled WGS sequence.
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; 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; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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 {ECO:0000256|HAMAP-Rule:MF_00473};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473}.
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 195
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 321
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 353 AA; 37626 MW; 17213CCCBC1FF5E4 CRC64;
MAEALTGLDP ETTLVVVVSK TFTTQETLAN AEAAKAWLTA ALPAEGMTKH FIGVTAAPDK
AAAFGCGRTF AFRDWVGGRY SLWSAVSLSC GIALGWDVFE AMLAGAAAMD DHFVSAPLEQ
NAPILLALAQ VFNVDGLNRP ARTVAPYAHA LRRLPSFLQQ LEMESNGKRV HRDGTPVTRQ
TCPVVFGEPG TNGQHAFFQQ IHQGPQIVPA EFVIVAKTHA DAPESPLWSN ALAQGQALML
GKTTEAAKAE GLAQGLSEEE AARLAPHRTF TGNRPSTAIV MDRLTPETLG ALLALYEHKT
FVEGVIWDIN SFDQWGVELG KVLARAILKD VDAGGPSADL DPSTAGLMTR LMG
//
