ID   G6PI_LARHH              Reviewed;         552 AA.
AC   C1DAI5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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};
GN   OrderedLocusNames=LHK_02316;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA   Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA   Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO75300.1; -; Genomic_DNA.
DR   RefSeq; WP_012697786.1; NC_012559.1.
DR   AlphaFoldDB; C1DAI5; -.
DR   SMR; C1DAI5; -.
DR   STRING; 557598.LHK_02316; -.
DR   GeneID; 75110974; -.
DR   KEGG; lhk:LHK_02316; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_4; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002010; 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   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; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..552
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_1000135533"
FT   REGION          525..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        357
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        388
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   552 AA;  61887 MW;  0C2EFE71B2A2A249 CRC64;
     MRFQSINEIN LTSVWAQLHL HQRSTRHVEM RDLFEAESDR FLNFSIDLNG FLLDFSKNRI
     TGRSLDLLVE LSKVAGLSDW VEAARLGEQI NTSEHRAVMH FALRASVDDV YSVDGQNVVP
     VVHRELRRCF DFSEKIRQKI WCGFNGSPIR DVVNIGIGGS DLGPRLAVQA LHPYALSDIR
     VHFVSNLDGA DLAQTLEGLD QATTLFIVSS KSFSTPETLD NAYAAKAWFL QKAQGSDVSK
     HFVAISSNVE AVKDFGIAPE QMFRFWDWVG GRYSVWSAIG LSVMIAIGER HFRAFLDGAR
     EMDQHFFTAP HEKNIPVVMA LLGVWYNTFY GAHTHAIMPY AHGLARLPAY LQQLDMESNG
     KRVGRFGEML DFDTGPVVWG EVGVNSQHAF FQLLHQGTRL VPCDFILPLR SHYAIGQHHQ
     QLVANCLAQT EALMRGKTDT EVLEELQAAG VTGELLDALL PQKVFPGNQP SNTIVIDELS
     PHFLGMLLAA YEHKVFVQGV IWGINSFDQW GVEYGKQLAK RIAPELASTK PPKHDSSTNA
     LIERYRTRGC RS
//