ID L8DLM2_9NOCA Unreviewed; 549 AA.
AC L8DLM2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=RHODMAR_4270 {ECO:0000313|EMBL:CCQ17655.1};
OS Rhodococcus sp. AW25M09.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ17655.1, ECO:0000313|Proteomes:UP000011207};
RN [1] {ECO:0000313|EMBL:CCQ17655.1, ECO:0000313|Proteomes:UP000011207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ17655.1,
RC ECO:0000313|Proteomes:UP000011207};
RA Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA Smalaas A.O., Altermark B.;
RT "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL Submitted (DEC-2012) 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}.
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:CCQ17655.1}.
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DR EMBL; CAPS01000116; CCQ17655.1; -; Genomic_DNA.
DR RefSeq; WP_008719086.1; NZ_CAPS01000116.1.
DR AlphaFoldDB; L8DLM2; -.
DR STRING; 1268303.RHODMAR_4270; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000011207; 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}.
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 384
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 510
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 549 AA; 59232 MW; 530B40CE8D3F4B4E CRC64;
MSVDITGTDA WQKLTDHHST IADTHLRTLF ADDADRARTF TLDAADLHVD YSKHRITRET
IELLVELART ADVEGKRDAM FAGEHINTSE DRAVLHTALR LPADASLTVD GQDVVADVHE
VLTAMGEFTD RVRSGEWVGA TGAKISTVVN IGIGGSDLGP VMVYDALRHY ADAGISAKFV
SNVDPADLVG ALDGLDPAST LFIIASKTFS TLETLTNATA ARRWLVDALG EDAVAKHFVA
VSTNAERVAD FGIDTANMFG FWDWVGGRYS VDSAIGLSVM AVVGKEAFGE FLAGFHRIDE
HFRTTPLAEN APVLLGLIGL WYSSFFGAET RAVLPYSNDL SRFAAYLQQL TMESNGKSVK
ADGSPVTTPT GEIFWGEPGT NGQHAFYQLL HQGTRLVPAD FIGFAEPTDD LPTRDGSGSM
HDLLMSNFFA QTKVLAFGKT AEEIAAEDTP ADVVPHKVMP GNRPSTSILA PTLTPSVVGQ
LIALYEHQVF VEGVIWGVDS YDQWGVELGK TQAIELTPVL TDAEAPAAQS DSSTDALVRW
YRAQRGRAV
//
