ID A0A0R0LJ32_9PROT Unreviewed; 525 AA.
AC A0A0R0LJ32;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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_1 {ECO:0000313|EMBL:KRH79047.1};
GN Synonyms=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN ORFNames=FERRO_01080 {ECO:0000313|EMBL:KRH79047.1};
OS Ferrovum sp. JA12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=1356299 {ECO:0000313|EMBL:KRH79047.1, ECO:0000313|Proteomes:UP000050960};
RN [1] {ECO:0000313|EMBL:KRH79047.1, ECO:0000313|Proteomes:UP000050960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA12 {ECO:0000313|EMBL:KRH79047.1,
RC ECO:0000313|Proteomes:UP000050960};
RA Poehlein A., Ullrich S.R., Tischler J.S., Schloemann M., Muehling M.,
RA Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain JA12.";
RL Submitted (SEP-2015) 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:KRH79047.1}.
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DR EMBL; LJWX01000001; KRH79047.1; -; Genomic_DNA.
DR RefSeq; WP_056928941.1; NZ_LJWX01000001.1.
DR AlphaFoldDB; A0A0R0LJ32; -.
DR STRING; 1356299.FERRO_01080; -.
DR PATRIC; fig|1356299.4.peg.108; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000050960; 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 343
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 374
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 488
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 525 AA; 56468 MW; 7A1B6CD5A4677772 CRC64;
MADLDPQTTP AWQALERLAG RYALGFDLRE AFAAEPNRFQ QHSVRAPHML VDLSKNLWDE
PVVEQLLALA MQMGLPERRN QLLNGEIVNQ TEHQAALHAS LRLAFTSGSE PASPAMAQHC
ADLSAMLAMA ETIRADATVH DVVHIGIGGS SLGPELALQA LRPYWRTQQR IHVVSNLDGH
DLAETLAQCH PAHTLFIAAS KSWSTFETLQ NLRSASGWLR QSGINPADRV VAITAKPNAA
QAAGLKHILR MPADLGGRYS VWSAVGLPVA VAIGEAGFRE LLAGAAAMDA HFAQAPLAQN
APVLLGLLDV WYSSFLHMPS RCVAPYHHRL RRLPAYLQQL DMESNGKTVR QNGDAVGYAT
GMALWGEAGT NGQHAFFQWL HQGAQRTPVE FVAARQAEHA LPGHHTPLLA NAVAQAQALM
LGSKAGPGQL TGHQDFPGNR PSTFLLLDGP LSPPALGALL ALYEHRTFVS GVVWGINSFD
QWGVELGKLL AKDILQRVPG GHWQGLDAST AGLLNAACVA SEAHS
//
