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Database: UniProt
Entry: A0A1J4P2M2_9ACTN
LinkDB: A0A1J4P2M2_9ACTN
Original site: A0A1J4P2M2_9ACTN 
ID   A0A1J4P2M2_9ACTN        Unreviewed;       497 AA.
AC   A0A1J4P2M2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   ORFNames=WN71_004265 {ECO:0000313|EMBL:OIJ69007.1};
OS   Streptomyces mangrovisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ69007.1, ECO:0000313|Proteomes:UP000034196};
RN   [1] {ECO:0000313|EMBL:OIJ69007.1, ECO:0000313|Proteomes:UP000034196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
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}.
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:OIJ69007.1}.
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DR   EMBL; LAVA02000010; OIJ69007.1; -; Genomic_DNA.
DR   RefSeq; WP_046584707.1; NZ_LAVA02000010.1.
DR   AlphaFoldDB; A0A1J4P2M2; -.
DR   STRING; 1428628.WN71_004265; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000034196; 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   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
DR   InterPro; IPR035482; SIS_PGI_2.
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:UP000034196}.
FT   NON_TER         497
FT                   /evidence="ECO:0000313|EMBL:OIJ69007.1"
SQ   SEQUENCE   497 AA;  55033 MW;  63C89BEBA806C0D5 CRC64;
     MNADGRTRLD QRPEWTALTE HREALGDVQL RELFDADPER GERCTLQVGD LHIDYSKHLV
     TDDTLRLLRE LAAATDVFGL RDAMFRGEKI NTTEDRAVLH TALRAPRDAV VEVDGQNVVP
     GVHAVLDKMA HFAERVRSGA WTGHTGKRIK NVVNIGIGGS DLGPAMAYEV LRSYTDRGLT
     VRFVSNVDGA DLHEAVRDLD AAETLFIVAS KTFTTIETIT NATSAREWLL GELKAGQEAV
     AQHFVALSTN EDKVTGFGID PANMFEFWDW VGGRYSYDSA IGLSLMIAIG PERFREMLDG
     FHLVDEHFRT APAEANVPLL MGLLGIWYGN FHDAQSHAVL PYSHYLSKFT AYLQQLDMES
     NGKYVGRDGR EVDWQTGPVV WGTPGTNGQH AYYQLIHQGT KLIPADFIGF ARPVDDLLPG
     FVAQHDLLMA NFFAQTQALA FGKTPEEVRA EGVPEELVPH KTFKGNHPTT TVLAEALTPS
     VLGQLIALYE HKVFVQG
//
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