ID   G6PI_CUTAK              Reviewed;         560 AA.
AC   Q6A5X5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=PPA2131;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT83838.1; -; Genomic_DNA.
DR   RefSeq; WP_002530768.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A5X5; -.
DR   SMR; Q6A5X5; -.
DR   EnsemblBacteria; AAT83838; AAT83838; PPA2131.
DR   KEGG; pac:PPA2131; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000603; 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.
FT   CHAIN           1..560
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180707"
FT   ACT_SITE        369
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        524
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   560 AA;  61457 MW;  7DB374E911211615 CRC64;
     MPTLIDATST PAWGTLSGLK SRFADGPHKL RRLFDADPHR AERYTLDVAD LHVDLSKNLL
     TDEIRDALLE LAAQMRVTER RDAMYAGEHI NVTEDRAVLH TALRRSRTDE LHVDGQDAVA
     DVHEVLDKIY AFADKVRSGE WKGVTGKPIR TVINVGIGGS DLGPVMAYEA LKPYVKDGLE
     CRFISNIDPT DAAVKTADLD PETTLVIIAS KTFTTLETLT NARCVRAWLL DGLVAAGAIS
     DTEQARRDAV AKHFVAVSTA LDKVEEFGID PVNAFGFWSW VGGRYSVDSA VGTSLAVAIG
     PKGFEDFLAG FHAVDEHFAT AEPERNVPLF MGLLNIWYTN FWDAHSHAVL PYSQYLHRFP
     AYLQQLTMES NGKSVRWDGS AVTTDTGEIF WGEPGTNGQH AFYQLIHQGT RVIPADFIAV
     ANPVHPTKDG GTDVHELFLS NFFAQTAALA FGKTADEVRA EGTDEAIVPA RVFAGDRPTT
     SIMADELSPK VLGELIALYE HITFVQGVVW GIDSFDQWGV ELGKKLALQI APAVSGNDEA
     LATQDPSTQG LVTWYREHRR
//