ID   G6PI4_RHOJR             Reviewed;         559 AA.
AC   Q0RUR2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Glucose-6-phosphate isomerase 4 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI 4 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase 4 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI 4 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase 4 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI 4 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi4 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   OrderedLocusNames=RHA1_ro11327;
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL3.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00473}.
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DR   EMBL; CP000434; ABH00974.1; -; Genomic_DNA.
DR   RefSeq; WP_011600599.1; NC_008271.1.
DR   AlphaFoldDB; Q0RUR2; -.
DR   SMR; Q0RUR2; -.
DR   STRING; 101510.RHA1_ro11327; -.
DR   EnsemblBacteria; ABH00974; ABH00974; RHA1_ro11327.
DR   KEGG; rha:RHA1_ro11327; -.
DR   PATRIC; fig|101510.16.peg.9135; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   OMA; VERCKAM; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008710; Plasmid pRHL3.
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; PTHR11469; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SSF53697; 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; Gluconeogenesis; Glycolysis; Isomerase; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..559
FT                   /note="Glucose-6-phosphate isomerase 4"
FT                   /id="PRO_0000252640"
FT   ACT_SITE        356
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   559 AA;  60664 MW;  F420E63665A92866 CRC64;
     MTAQHSDITA TSAWQKLHAH RDETSALTIR ELFAADTERG RELTLTAGEL YIDYSKQRVS
     RHTLALLVEL ARAAGVEERR DAMFRGERIN TSEDRAVLHT ALRLPAHASL RVDGHDVVAD
     VHRVLARMGV FSDRLRSGEW RGATGRPIMT VVNIGIGGSD LGPHMVYRAL RHYADSGISV
     RFISNVDPSD LVATLADLDP STTLFIVASK TFSTLETLTN AANARRWVTS ALGEQAVARH
     FVAVSTNAER VAAFGIDTEN MFGFWDWVGG RYSVGSAVGL AVMVAIGKDS FEEFLDGFHT
     IDRHFADTPL EDNAPAILAL LGVWYSNFFG AETRAILPYS NDLGRFPAYL QQLAMESNGK
     SVRADGSPIG TTTGAVFWGE PGSNGQHAFY QLLHQGTRLV PADFIGFAEP THDLPAADGA
     GSMHNILMSN LFAQSRVLAF GKTPEELTRE DTAPDLIAHK TMPGNQPSTT ILAPRLTPSV
     LGQLIALYEH QVFVEGIIYG IGSFDQWGVE LGKTQALELE PALSSGNGSL PSDLDSSTAS
     MIRWYHGVRA HGTATVGRP