ID A0A1G8EIW0_9MICC Unreviewed; 545 AA.
AC A0A1G8EIW0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=SAMN04488693_102131 {ECO:0000313|EMBL:SDH69659.1};
OS Arthrobacter subterraneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=335973 {ECO:0000313|EMBL:SDH69659.1, ECO:0000313|Proteomes:UP000199258};
RN [1] {ECO:0000313|EMBL:SDH69659.1, ECO:0000313|Proteomes:UP000199258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP_1H {ECO:0000313|EMBL:SDH69659.1,
RC ECO:0000313|Proteomes:UP000199258};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
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DR EMBL; FNDT01000002; SDH69659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8EIW0; -.
DR SMR; A0A1G8EIW0; -.
DR STRING; 335973.SAMN04488693_102131; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000199258; Unassembled WGS sequence.
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 InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
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; 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:UP000199258}.
SQ SEQUENCE 545 AA; 56104 MW; 4567F8644FD56566 CRC64;
MATLFVNASG AAAEAIERAM PELVEERVAS RIMAKDSTLW GPESESEASV RLGWVDLIEA
SRALLPDIAQ LRSDLHGDGV NHIVLCGMGG SSLAPEVITR SAGVELTVLD STDPAQVRAA
LADRIGSTAV VVSSKSGSTV ETDSQRRAFE QAFADAGVDP KSRIIIVTDP GSPLDESARA
AGYRAVFTAD PTVGGRYSAL TAFGLVPSGL AGADLASLLD DAESISEFLT DDDAGNVGLR
LGAVLGGTLP LRDKIVFADE GSGIVGLGDW VEQLIAESTG KLGTGVLPVV VEQDAPELSS
GAPDVLAVHL VSPESTTEPE GDSIAVGGSL GSQLLAWEFA TAVAGRLLGI NPFDQPDVEA
AKQAARGLLD AQPESVPANF VDGAVEVRGS TALLGTASTL GEALESLFGA LESNGYLAVQ
AYLDRIAEAP LAGIRPALAG ITGRPVTFGW GPRFLHSTGQ FHKGGTPVGV FLQITGATTE
DLAIPERPFS FGELITAQAA GDAQVLQDAG RPVLRLHLAD RAEGLRQLQD VISHLSGQSA
ENGNG
//
