G6PI_PROMP
ID G6PI_PROMP Reviewed; 526 AA.
AC Q7V1I1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PMM0890;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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}.
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DR EMBL; BX548174; CAE19349.1; -; Genomic_DNA.
DR RefSeq; WP_011132523.1; NC_005072.1.
DR AlphaFoldDB; Q7V1I1; -.
DR SMR; Q7V1I1; -.
DR STRING; 59919.PMM0890; -.
DR EnsemblBacteria; CAE19349; CAE19349; PMM0890.
DR KEGG; pmm:PMM0890; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_033288_0_0_3; -.
DR OMA; CPAYAYG; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001026; 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 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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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.
FT CHAIN 1..526
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180706"
FT ACT_SITE 323
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 352
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 454
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 526 AA; 59307 MW; A785CE626C2AD6CA CRC64;
MNNDFNSWDK YCNYLWFDKQ VNIWLDISKI NFTLDQISSL ENKFKKVFSA LKELEAGAIS
NIDEKRQVGH YWLRNPSVAP SNLIKDAINN EIRDISEFGE KILEGKITNN KNQKFTNVLW
IGIGGSGLGP LLITEALQEN SCGLNFSYID NIDPFLISEK LDELSDKLAT TLFVVVSKSG
GTPEPKIAMN IIKKHVENKN LDWNSNAIAI TMKDSQLYKK AQLENWLKIF NLPDWVGGRT
SITSSVGLLP LALINRDVSE FIKGAAIMDD LTRIPNIKDN PAALLSSAWF FSGDGIGKRD
MVVLPYRDRL QVFSKYLQQL VMESLGKKFN RKGEIVHQGI SVFGNKGSTD QHAYVQQLRD
GIDNFFCVFI ELLDTPNSNF YFDSENPKEF LSGFLQGTRS ALSNENRQSI TITLDKLSCL
TLGALIALFE RAVSFYAELV DINAYDQPGV EAGKKAAAEI IDYQKQVTEI FNNGEELSIK
EITSLLRNSS AEPIFFIIRQ MCFGNDDYLI NGDWSKPSTI RIKKIS