G6PI_LACLA
ID G6PI_LACLA Reviewed; 448 AA.
AC P81181;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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}; Synonyms=pgiA;
GN OrderedLocusNames=LL2168; ORFNames=L0012;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=9169021; DOI=10.1006/abbi.1997.9959;
RA Nomura M., Nakajima I., Matsuzaki M., Kimoto H., Suzuki I., Aso H.;
RT "The N-terminal sequence of Lactococcus lactis phosphoglucose isomerase
RT purified by affinity chromatography differs from the other species.";
RL Arch. Biochem. Biophys. 341:315-320(1997).
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, ECO:0000305}.
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DR EMBL; AE005176; AAK06266.1; -; Genomic_DNA.
DR PIR; H86895; H86895.
DR RefSeq; NP_268325.1; NC_002662.1.
DR RefSeq; WP_010906353.1; NC_002662.1.
DR AlphaFoldDB; P81181; -.
DR SMR; P81181; -.
DR STRING; 272623.L0012; -.
DR PaxDb; P81181; -.
DR EnsemblBacteria; AAK06266; AAK06266; L0012.
DR GeneID; 60356170; -.
DR GeneID; 61110492; -.
DR GeneID; 66443157; -.
DR KEGG; lla:L0012; -.
DR PATRIC; fig|272623.7.peg.2328; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_0_1_9; -.
DR OMA; CPAYAYG; -.
DR BioCyc; MetaCyc:MON-13046; -.
DR SABIO-RK; P81181; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002196; 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; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9169021"
FT CHAIN 2..448
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180660"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 425
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 448 AA; 49595 MW; 582AD419B00BB5C2 CRC64;
MAHIKFDYSK LTPFVAENEL DEIQWQIDGA AKLLHEGKGA GSDYIGWLDL PEDYDKEEFA
RIQKAAKKIQ SDSEVLIVIG IGGSYLGARA AIDFLSNSFV NLQTAEERKA PRILYAGNSI
SSSYLADLVD YVADKDFSVN VISKSGTTTE PAIAFRVFEE MLVKKYGREE ANKRIYATTD
KEKGAVKVNA DANNWETFVV PDSVGGRFSV LTAVGLLPIA ASGADITALM EGANAARKEY
TSTNVHENDA YAYAALRNIL YRKGKFSEIL INYEPSLQYF SEWWKQLAGE SEGKDQKGIY
PTSANFSTDL HSLGQWIQEG TRTVFETAIR IEKPRKNINI PELDADLDGL GYLQGKDVDF
VNKKAADGVL LAHTDGNVPN MIVTLPEQDE FTLGYAIYFF ELAIGVSGYL NGINPFNQPG
VEAYKKNMFA LLGKPGFEEL SKELNDRL
