G6PI_BACAN
ID G6PI_BACAN Reviewed; 450 AA.
AC Q81K75; Q6HRM8; Q6KKZ2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473};
GN OrderedLocusNames=BA_5130, GBAA_5130, BAS4767;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP28802.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34259.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57060.1; -; Genomic_DNA.
DR RefSeq; NP_847316.1; NC_003997.3.
DR RefSeq; WP_000103657.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_031010.1; NC_005945.1.
DR PDB; 3IFS; X-ray; 2.00 A; A/B/C/D/E/F=1-450.
DR PDBsum; 3IFS; -.
DR AlphaFoldDB; Q81K75; -.
DR SMR; Q81K75; -.
DR IntAct; Q81K75; 1.
DR STRING; 260799.BAS4767; -.
DR DNASU; 1084495; -.
DR EnsemblBacteria; AAP28802; AAP28802; BA_5130.
DR EnsemblBacteria; AAT34259; AAT34259; GBAA_5130.
DR GeneID; 45024758; -.
DR KEGG; ban:BA_5130; -.
DR KEGG; bar:GBAA_5130; -.
DR KEGG; bat:BAS4767; -.
DR PATRIC; fig|198094.11.peg.5091; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_0_1_9; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q81K75; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
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 HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..450
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180584"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3IFS"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3IFS"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 150..167
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 325..334
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 359..376
FT /evidence="ECO:0007829|PDB:3IFS"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 391..412
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 423..433
FT /evidence="ECO:0007829|PDB:3IFS"
FT HELIX 439..449
FT /evidence="ECO:0007829|PDB:3IFS"
SQ SEQUENCE 450 AA; 50345 MW; A8F91E74160A80D9 CRC64;
MSTHVTFDYS KALSFIGEHE ITYLRDAVKV THHAIHEKTG AGNDFLGWVD LPLQYDKEEF
ARIQKCAEKI KNDSDILLVV GIGGSYLGAR AAIEMLNHSF YNTLSKEQRK TPQVLFVGQN
ISSTYMKDLM DVLEGKDFSI NVISKSGTTT EPALAFRIFR KLLEEKYGKE EARKRIYATT
DKARGALKTL ADNEGYETFV IPDDVGGRFS VLTPVGLLPI AVSGLNIEEM MKGAAAGRDD
FGTSELEENP AYQYAVVRNA LYNKGKTIEM LINYEPALQY FAEWWKQLFG ESEGKDQKGI
FPSSANFSTD LHSLGQYVQE GRRDLFETVL KVGKSTHELT IESEENDLDG LNYLAGETVD
FVNTKAYEGT LLAHSDGGVP NLIVNIPELN EYTFGYLVYF FEKACAMSGY LLGVNPFDQP
GVEAYKKNMF ALLGKPGFEE LKAELEERLK
