ID A0A1M7RIN8_9ACTN Unreviewed; 545 AA.
AC A0A1M7RIN8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN ORFNames=SAMN05443668_1146 {ECO:0000313|EMBL:SHN46163.1};
OS Cryptosporangium aurantiacum.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=134849 {ECO:0000313|EMBL:SHN46163.1, ECO:0000313|Proteomes:UP000184440};
RN [1] {ECO:0000313|EMBL:SHN46163.1, ECO:0000313|Proteomes:UP000184440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46144 {ECO:0000313|EMBL:SHN46163.1,
RC ECO:0000313|Proteomes:UP000184440};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000256|HAMAP-Rule:MF_00473}.
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|ARBA:ARBA00029321,
CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC ECO:0000256|RuleBase:RU000612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
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DR EMBL; FRCS01000014; SHN46163.1; -; Genomic_DNA.
DR RefSeq; WP_073262943.1; NZ_FRCS01000014.1.
DR AlphaFoldDB; A0A1M7RIN8; -.
DR STRING; 134849.SAMN05443668_1146; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000184440; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
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; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473};
KW Reference proteome {ECO:0000313|Proteomes:UP000184440}.
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 388
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 508
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 545 AA; 59643 MW; 097E60124DD4BFE0 CRC64;
MSPKTVEIDA TPEWAAAGEH AARLRDTHLR DLFAADADRA DRLTVEAAGL IADYSKHRVD
DDALAALFAL ARAADVEGHR DAMLRGEKIN TTENRAVLHT ALRAPRDAEI IVDGENVVPQ
VHEVLDRMAS FSDRVRSGEW VGSTGQRIRT VVNIGIGGSD LGPRMAYEAL KPYADPEIAC
RFVSNVDGDD LSANLTGLDA EQTLFIVASK TFTTLETMTN ARAARDWLVG QLGDKADVAK
HFVAVSTNLK AVEEFGIDPV NTFGFWDWVG GRYSFDSAIG LSLMVAIGPN GFRELLAGMR
AIDEHFASAP LEQNLPVILG VLGVWYREFF DAQSHAVLPY AHYLSRFTDY LQQLDMESNG
KRVRRDGTPV AYRTGPIVWG TPGTNGQHAY YQLIHQGTTL IPVDFLAFLH PAHEVGNQHD
LLTANVLAQA EALAFGKTAE QVAAEGVAAE LVPHRTFPGN HPSTTLVVEK LTPRTLGALV
ALYEHKVFVQ GAIWQINSFD QWGVELGKAL AQRIVPELEA DAEPELNHDS STNALIRRHR
AARRG
//
