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Database: UniProt
Entry: A0A1L7F6P1_9PSEU
LinkDB: A0A1L7F6P1_9PSEU
Original site: A0A1L7F6P1_9PSEU 
ID   A0A1L7F6P1_9PSEU        Unreviewed;       543 AA.
AC   A0A1L7F6P1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN   ORFNames=UA75_12490 {ECO:0000313|EMBL:APU20510.1};
OS   Actinoalloteichus sp. GBA129-24.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU20510.1, ECO:0000313|Proteomes:UP000185506};
RN   [1] {ECO:0000313|EMBL:APU20510.1, ECO:0000313|Proteomes:UP000185506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GBA129-24 {ECO:0000313|EMBL:APU20510.1,
RC   ECO:0000313|Proteomes:UP000185506};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT   (=GBA129-24).";
RL   Submitted (JUN-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; CP016077; APU20510.1; -; Genomic_DNA.
DR   RefSeq; WP_075740399.1; NZ_CP016077.1.
DR   AlphaFoldDB; A0A1L7F6P1; -.
DR   STRING; 1612551.UA75_12490; -.
DR   KEGG; acti:UA75_12490; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000185506; 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   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}.
SQ   SEQUENCE   543 AA;  55508 MW;  054ACC3FF71CEEA7 CRC64;
     MTEVNNAAPS VVIADGPWAQ EAGELAERLA AEAVAGELTA GNPTLWGADA ESEAAVRLAW
     TTLPKTSRPL LGEIAALRGE LHAEGVDRVV LAGMGGSSLA PEVITAAAGV PLTVLDTTDP
     GQVADALAGD LSRTVLVVSS KSGSTVETDS HRRIFEHAFE AAGIPAASRI VVVTDPESPL
     ETAARAAGYR HVFRADPHVG GRYSALTAFG LVPAGLAGAD VAGLLAEAAS AAPTLAQDEP
     DNPALRLAGA FGAALARGAE KVVFADNDSG LPGFADWAEQ LIAESTGKNG TGLLPVVVEN
     VSAPGFVDAG DDATTVALGS PDSAATLTVS GSLGASFLLW EYATAIAGRL LGINPFDQPD
     VEAAKTAARS LLDSSDGSAT PTPLLVDGPV EAYVAGSWQP PEGAGLDELI ASFVAAVPET
     GYLSLQAYLD REQDASAAVL RRELARNTGV QTTFGWGPRF LHSTGQYHKG GHQNGAFLQI
     TGAAEEDLAV PDRPYTLATL QLAQALGDGT VLADRGRPVL RLHLTDRLAG LARLAEAVQG
     VSR
//
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