ID A0A1I5U4Q6_9BACT Unreviewed; 550 AA.
AC A0A1I5U4Q6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05444277_10365 {ECO:0000313|EMBL:SFP90250.1};
OS Parafilimonas terrae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Parafilimonas.
OX NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFP90250.1, ECO:0000313|Proteomes:UP000199031};
RN [1] {ECO:0000313|EMBL:SFP90250.1, ECO:0000313|Proteomes:UP000199031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28286 {ECO:0000313|EMBL:SFP90250.1,
RC ECO:0000313|Proteomes:UP000199031};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00029321,
CC ECO:0000256|HAMAP-Rule:MF_00473, 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|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC ECO:0000256|RuleBase:RU000612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOXQ01000003; SFP90250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5U4Q6; -.
DR STRING; 1465490.SAMN05444277_10365; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000199031; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199031}.
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 388
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 550 AA; 62658 MW; 877FC54EDF9598CB CRC64;
MLPKINPANT QAWLLLTKHQ SEEMRHITMK RLFAEDEDRF NKFSIKFGDI LFDYSKNIIV
QKTLQLLLQL ADDCKVKEAI TEMFNGDKIN ETENRSVLHT ALRNFSGEPV LSDGKDVMPD
VQRVQQQMKA FCEKIHSGEW KGYSGKKIKY IVNIGIGGSD LGPVMVTEAL KPYWVEGIQP
YFVSNIDGTH IAETLKKITP DETLFLIASK TFTTQETMTN AHTAREWFLQ SAKDEQHVAK
HFAALSTNEK EVKKFGIDTV NMFEFWDWVG GRYSLWSAIG LSIALTIGYN NFEELLKGGY
ETDVHFKTTA FDKNIPILMA LIGIWYTNFF KAQTEAILPY DQYMHRFAAY FQQGNMESNG
KYVNRNGSET NYATGPVIWG EPGTNGQHAF YQLIHQGTLL IPCDFIAPAV SHNPIGDHHL
KLLSNFFAQT EALMKGKDEA EVREELKKEN KSPEEIKRLV PFKVFKGNKP TNSFLIKEIT
PKTLGNLIAL YEHKIFVQGI IWNIFSFDQW GVELGKQLAS KVLPELENNN KITSHDSSTN
GLINAWKAMK
//
