ID A0A1H8XXF6_9PSEU Unreviewed; 539 AA.
AC A0A1H8XXF6;
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=SAMN04489732_109149 {ECO:0000313|EMBL:SEP43978.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP43978.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP43978.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP43978.1,
RC ECO:0000313|Proteomes:UP000198582};
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; FOEF01000009; SEP43978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8XXF6; -.
DR STRING; 394193.SAMN04489732_109149; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000198582; 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; 2.
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:UP000198582}.
SQ SEQUENCE 539 AA; 55547 MW; DB812999A31D89F3 CRC64;
MTGDETGVEI VDAELAGKAA PLVERLVADQ AATKLAANDA TLWGPDAESE ASIRLSWTSL
HKSSRPLIGE IEALRTELRG EGVDRVVLAG MGGSSLAPEV IAGTSEVALT VLDTTDPGQV
ADALAGDLER TVLVVSSKSG GTLETDSHRR IFAKAFADAG IDAARRIVVV TDPGSPFAEL
SEKEGYRKTF LADPHVGGRY SALTAFGLVP AGLAGADIAR LLDQAAAVAG VLGSDSADNP
AIKLAAAWAA AHEGGAEKVV LADTGSGIKG FPDWAEQLIA ESTGKLGTGL LPVAVEGPDA
PGFADAKSDA TPVAIGDAEG AAKIAVTGPL GAQFLLWEFA TALAGRLLGI NPFDQPDVEA
AKKAARALLD DPEKLKGGET ASNVDGAVEI FGSEGVVTEG KLADVLRAFF ASAPEHGYIA
VQAYLDRLDD ASTALLRGEV AKRTGLQTTF GWGPRFLHST GQYHKGGHQN GNFLQVTGAV
AEDLEVPDRP YTLGQLQHAQ ALGDGQVLAE HGRPVLRLHL TDRAAGLAEL VRAVQEVGA
//
