G6PI_PROMM
ID G6PI_PROMM Reviewed; 551 AA.
AC Q7V7M6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 92.
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=PMT_0714;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE20889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX548175; CAE20889.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q7V7M6; -.
DR SMR; Q7V7M6; -.
DR STRING; 74547.PMT_0714; -.
DR EnsemblBacteria; CAE20889; CAE20889; PMT_0714.
DR KEGG; pmt:PMT_0714; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_033288_0_0_3; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001423; 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; Reference proteome.
FT CHAIN 1..551
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180705"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 378
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 480
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 551 AA; 60929 MW; B569FD6DC1F98AD0 CRC64;
MSRHFDRGSF RAVSDVHQLM SFPDFSASDA HVQWQRFNNL LWHHNDLGIW LDISRMHINA
EDFERLGPRF DQAFKAMQAL EQGAIANTDE QRMVGHYWLR QPQLAPDQEV CDHIAKEIDL
IETFGSNVIN GLIKAPNGKK FTDVLWIGIG GSGLGPLLMI RALQNAEQGL RFHFFDNVDP
DGMSRVLGNL GDALSTTLVV TVSKSGATPE PHLGMEQARQ RLEAMGGHWA GQAVAVTMLN
SQLDQLAQKE SWLKRFDMFD WVGGRTSITS AVGLLPAALI GCDIRAFLAG AAQMDEATRV
SDLHSNPASL MAAAWFVAGD GLGRRDMVVL PYRDRLEVFS RYLQQLVMES LGKRLDRDGN
VVHQGLAVYG NKGSTDQHAY VQQLRDGVDN FFATFIEVLE DVENIPAINN EHPGDFLDGF
LQGTRAALSQ GGRQSLTISM RRFDPRRLGA LVALFERAVG LYGELVNINA YHQPGVESGK
KAAAAILNLQ SRVEDLLADG VERSAGEIHQ VIGDGSEEAI FWIMRHLTAN KRGYVAEGDW
GIPTSLRFSK G