ID C9R8T7_AMMDK Unreviewed; 448 AA.
AC C9R8T7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN OrderedLocusNames=Adeg_1622 {ECO:0000313|EMBL:ACX52716.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52716.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX52716.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000612};
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|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
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DR EMBL; CP001785; ACX52716.1; -; Genomic_DNA.
DR RefSeq; WP_015739593.1; NC_013385.1.
DR AlphaFoldDB; C9R8T7; -.
DR STRING; 429009.Adeg_1622; -.
DR KEGG; adg:Adeg_1622; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_1_0_9; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000002620; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 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; 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; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW Reference proteome {ECO:0000313|Proteomes:UP000002620}.
SQ SEQUENCE 448 AA; 50270 MW; DC69F24CEF4B80A1 CRC64;
MLKVDVGHFL AGIEGELENY QEPFLRFQER LRSRTYPFTL SLEEGSKIPP MEAVAERLRN
SYETFLVLGI GGSSLGVKAL VQFLKGPYYN LAGSPRLLVL DNISPHLAQQ LTDLLDWRRT
GLIYISKSGS TPETAANFLY FYKLYREAGG KPQDLVFICD PGDNGMNRIA RELGAEVFHL
PPPLPGRYSV LSPVGLFPAA LLRIPGEELL EGARRVHEVL AAESPEANPL FLLGGGICYW
SARGKNIHVL FNYETLLSEF GFWFMQLWAE SLGKKLSLTG AEVRAGTTPL ACVGTTDQHS
LLQLFKEGPD DKIYGFVTIK EKPEVLLPSL FATEKEYAYF GGRTLGEQLA IEQLATEISL
VREGRPCYHV ATRDVSPASL GALFYFFEAL VVFVAECWQV NPFDQPGVEE GKQITYALMG
RQDYKARRPQ FEELVEEFTR RRQIYTIS
//
