ID W2F4I8_9ACTN Unreviewed; 537 AA.
AC W2F4I8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=MPTA5024_00275 {ECO:0000313|EMBL:ETK38136.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK38136.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK38136.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK38136.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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:ETK38136.1}.
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DR EMBL; AWEV01000006; ETK38136.1; -; Genomic_DNA.
DR AlphaFoldDB; W2F4I8; -.
DR STRING; 316330.MPTA5024_00275; -.
DR PATRIC; fig|316330.3.peg.51; -.
DR HOGENOM; CLU_036298_0_0_11; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000018869; 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:UP000018869}.
SQ SEQUENCE 537 AA; 56780 MW; A399721ED038A321 CRC64;
MTLGDEVESV ETVRDKLVAE GVPAALAAGD PSLWGPQAQP EATIRLGWLN LPQSSRELLP
EIDKLVERAR AEGLDHVVLA GMGGSSLAPE VICATYDVPL TVLDTTDPHQ VRRALSDRLE
RTLVVVASKS GGTIETDSHR RIYEKAFRDA GIDPATRIVV VTDPGSPLEQ AANEAGYPVV
LADPNVGGRY SALTAFGLVP SALAGADVRR LLDEAESVRA LLAQDAGNPG LDLGAVLGAE
ALRGRDKLIL RDGMSDITGL PDWIEQLIAE STGKEGKGVL PVVGAEAAED DDQYVVSIGP
DGGTAVDGPL GAQFLVWEYA TAIAGRAIGI NPFDQPNVAE SKENTTRILQ EAGDGPLPAG
TPLLTDGPVE VYGDVPGDPK NLADVLTWLL RAVPERGYLA IMAYLDREAA FDAATVGDAS
FEEMTETWAG ADVATLRALL DYRTDRPVTF GWGPRFLHST GQYHKGGPQD GVYLQITGAV
TDDVEVPGKP YTLGRLQLAQ ALGDLGALTS RGRPAVRLHL TDRVAGVRHL LSVAEEL
//
