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Database: UniProt
Entry: C0VZK3_9ACTO
LinkDB: C0VZK3_9ACTO
Original site: C0VZK3_9ACTO 
ID   C0VZK3_9ACTO            Unreviewed;       559 AA.
AC   C0VZK3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN   Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473,
GN   ECO:0000313|EMBL:EEH64122.1};
GN   ORFNames=HMPREF0044_0593 {ECO:0000313|EMBL:EEH64122.1};
OS   Gleimia coleocanis DSM 15436.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Gleimia.
OX   NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH64122.1, ECO:0000313|Proteomes:UP000010301};
RN   [1] {ECO:0000313|EMBL:EEH64122.1, ECO:0000313|Proteomes:UP000010301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH64122.1,
RC   ECO:0000313|Proteomes:UP000010301};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00029321,
CC         ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|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:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC       ECO:0000256|RuleBase:RU000612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEH64122.1}.
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DR   EMBL; ACFG01000029; EEH64122.1; -; Genomic_DNA.
DR   RefSeq; WP_006546053.1; NZ_DS999539.1.
DR   AlphaFoldDB; C0VZK3; -.
DR   STRING; 525245.HMPREF0044_0593; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000010301; Unassembled WGS sequence.
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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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 {ECO:0000256|HAMAP-Rule:MF_00473};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010301}.
FT   ACT_SITE        367
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        398
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        522
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   559 AA;  61320 MW;  5F3BC55B487AEDE0 CRC64;
     MKMVNPVNPT TTAAWKSLTE TAATFTPNMR QWFADNPNRA KEYTRTMADL HVDLSKNLLT
     DEILADLCTL ADEVNLRERI NAMFSGVHIN NTEDRAVLHT ALRKPAGTEL VVDGVEVVAD
     VHAELEKVYA FAEKVRSGEW KGVTGKRIET VVNIGIGGSD LGPVMVYEAL KPYAQAGLSA
     RYISNIDPTD AGEKTKDLDP ETTLVIVASK TFTTLETLTN ARVVREWLLS SLRARGVFEG
     DIDEAAAVRS HFVAVSTALD KVAAFGIDPV NAFGFWNWVG GRYSVDSAVG TSLAVVLGPD
     VFKEFLAGFH AVDEHFRTTE WSQNVPALMG LLNVWYVNFL DAHTHAVLPY AQFLSRFPAY
     LQQLTMESNG KSVTWAGEAV NYQTGEIFWG EPGTNGQHAF YQLIHQGTRI VPADFIAFAN
     PTWAFVDGEN DMHELFLGNF FAQTKALAFG KTAEEVRAEG TPEEIVPARV FAGNKPSTSI
     MAASLTPAVL GQLIALYEHI TFVQGIVWGV NSFDQWGVEL GKQLANQLTP AVAGDREVLA
     QQDPSTQGLI EFYLANRVK
//
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