ID A0A164C1Y4_9SYNE Unreviewed; 532 AA.
AC A0A164C1Y4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ECO:0000313|EMBL:KZR89629.1};
GN ORFNames=MITS9508_01235 {ECO:0000313|EMBL:KZR89629.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR89629.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR89629.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR89629.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZR89629.1}.
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DR EMBL; LVHU01000005; KZR89629.1; -; Genomic_DNA.
DR RefSeq; WP_067094698.1; NZ_LVHU01000005.1.
DR AlphaFoldDB; A0A164C1Y4; -.
DR STRING; 1801629.MITS9508_01235; -.
DR PATRIC; fig|1801629.3.peg.1315; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000076799; 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 HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
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; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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 330
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 359
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 461
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 532 AA; 58608 MW; 2450BD07D3E39690 CRC64;
MSFPDFSATD AQIQWQRFCD LLWHHEDLGM WLDVSRMHLN NAQLEELTPR LEKAFEAMKA
LENGAIANAD ENRQVGHYWL RHPQLAPDPE VGQHISTEID QIEQFGKAVI NGTIKSPTGQ
PFTDVLWIGI GGSGLGPLLM IRALQEKGVG LPFHFFDNVD PNGMSRVLAE LGDALRTTLV
VTVSKSGGTP EPHLGMEQAR HRLEAVGGQW SAQAVAITMA ESKLDQQALA EQWLQRFDMF
DWVGGRTSIT SAVGLVPGAL IGSDIRSFLA GASQMDEATR VNDVRRNPAA LMAAAWYSAG
GGKGKRDMVV LPYRDRLEVF SRYLQQLVME SLGKRLDRNG DVAHQGIAVY GNKGSTDQHA
YVQQLRDGVD NFFVTFIEVL RDVEDIPEIN GERPGDFLDG FVQGTRSALT EGGRQSLSIS
MRQFDARRLG ALIALFERAV GFYGELVNIN AYHQPGVEAG KKAAAAILKL QLQVEDVLSD
GVSRSVVEIQ QAIGEGSVEA VFWIVRHLTG NNRGYQAQGD WNKPATLRFS KC
//
