ID   G6PI4_RHOSR             Reviewed;         559 AA.
AC   Q0RUR2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Glucose-6-phosphate isomerase 4;
DE            Short=GPI 4;
DE            EC=5.3.1.9;
DE   AltName: Full=Phosphoglucose isomerase 4;
DE            Short=PGI 4;
DE   AltName: Full=Phosphohexose isomerase 4;
DE            Short=PHI 4;
GN   Name=pgi4; OrderedLocusNames=RHA1_ro11327;
OS   Rhodococcus sp. (strain RHA1).
OG   Plasmid pRHL3.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., 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   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GPI family.
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DR   EMBL; CP000434; ABH00974.1; -; Genomic_DNA.
DR   RefSeq; YP_709132.1; -.
DR   GeneID; 4226768; -.
DR   GenomeReviews; CP000434_GR; RHA1_ro11327.
DR   KEGG; rha:RHA1_ro11327; -.
DR   HOGENOM; Q0RUR2; -.
DR   OMA; Q0RUR2; DHINTTE.
DR   BioCyc; RSP101510:RHA1_RO11327-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_00473; -; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   PANTHER; PTHR11469; G6P_Isomerase; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Plasmid.
FT   CHAIN         1    559       Glucose-6-phosphate isomerase 4.
FT                                /FTId=PRO_0000252640.
FT   ACT_SITE    356    356       Proton donor (By similarity).
FT   ACT_SITE    387    387       By similarity.
FT   ACT_SITE    513    513       By similarity.
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
//