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Database: UniProt
Entry: D3LN52_MICLU
LinkDB: D3LN52_MICLU
Original site: D3LN52_MICLU 
ID   D3LN52_MICLU            Unreviewed;       533 AA.
AC   D3LN52;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN   Name=pgi {ECO:0000313|EMBL:EFD50999.1};
GN   ORFNames=HMPREF0569_0810 {ECO:0000313|EMBL:EFD50999.1};
OS   Micrococcus luteus SK58.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Micrococcus.
OX   NCBI_TaxID=596312 {ECO:0000313|EMBL:EFD50999.1, ECO:0000313|Proteomes:UP000002933};
RN   [1] {ECO:0000313|EMBL:EFD50999.1, ECO:0000313|Proteomes:UP000002933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK58 {ECO:0000313|EMBL:EFD50999.1,
RC   ECO:0000313|Proteomes:UP000002933};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (NOV-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|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}.
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:EFD50999.1}.
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DR   EMBL; ADCD01000046; EFD50999.1; -; Genomic_DNA.
DR   RefSeq; WP_002855641.1; NZ_ADCD01000046.1.
DR   AlphaFoldDB; D3LN52; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000002933; 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}.
SQ   SEQUENCE   533 AA;  55122 MW;  B23BC723AF0B2077 CRC64;
     MSTLGLTATG AALEAIDRHL PALLQDRVAS RLGAQDADLW GAPARDEAAK RLGWIDLFED
     SRALVPHIAQ LTRELRAEGV DRVVLAGMGG SSLAPEVIAA TAGVELEVLD STDPLQVSRA
     LERDLERTVL VVSSKSGSTV ETDSQRRVVE AAFRDAGIDP RTRLVAVTDP GSPLHAACES
     AGWRAVFTAD PTVGGRFSAL AAFGLVPTGL AGVDVAALLD DAEAVLDLLT ADDEDNPGLQ
     LGAALGGTQP LRDKLVFADH GSGIAGLPAW IEQLIAESTG KDGTGLLPVV VAPGDPETAW
     DAPDLLQVQL VGEDDVAAPG HGVQVAGSLG AQLLLWEVAT AVAGRLLGIN PFDQPDVEAA
     KAAARTLLDG PAAERTADGE VEGVEVSGPA SVTSAPDLAG VLRATAALVP EDGYLAVHAY
     LSRHDDAELE GLRADLADLV GRPVTFGWGP RFLHSTGQFH KGGPAVGVFL QITGDAGLDL
     EVPGRPFSLG RLIAAQAAGD ARVLGDLDRP VVTLHLRRRD AGIEALRSAV RGR
//
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