ID A0A132MH29_HYDSH Unreviewed; 444 AA.
AC A0A132MH29;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=SA87_01355 {ECO:0000313|EMBL:OAR03406.1};
OS Hydrogenibacillus schlegelii (Bacillus schlegelii).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family X. Incertae Sedis; Hydrogenibacillus.
OX NCBI_TaxID=1484 {ECO:0000313|EMBL:OAR03406.1, ECO:0000313|Proteomes:UP000243024};
RN [1] {ECO:0000313|EMBL:OAR03406.1, ECO:0000313|Proteomes:UP000243024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA 48 {ECO:0000313|EMBL:OAR03406.1,
RC ECO:0000313|Proteomes:UP000243024};
RA Hemp J.;
RT "Draft genome sequence of Hydrogenibacillus schlegelii DSM 2000.";
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}.
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:OAR03406.1}.
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DR EMBL; JXBB01000060; OAR03406.1; -; Genomic_DNA.
DR RefSeq; WP_066203128.1; NZ_JYFD01000225.1.
DR AlphaFoldDB; A0A132MH29; -.
DR STRING; 1484.SA87_01355; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000243024; 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 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000243024}.
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 414
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 444 AA; 48331 MW; E22161CD808EF938 CRC64;
MRPIRLDAAS YRPFVAPEEV ERAADVVRSL HPTLVERRSE SAMVGWLDYP SRIGEETLGG
VEAIAERVRR DADVFFVVGV GGSSLGARAA LEFLGRDAAA PEIRFVGEDL SPTSLVEALE
AVRTRRVVLN VVSKSGTTTE PAVAFRLLRE TLETAVGPAE ARRRIIATTD PSGGALRAMA
EAEGWTSFDI PRDVGGRFSV LTPVGLLPMA VAGIDVRRVL AGARALMAAP EGTDPAADDP
NRYAMLRHIL YLKGYAIELF VGFTPRLSGV GAWLRQLFAE SEGKNGRGIF PVTGKYTTDL
HSIGQYVQDG RRLLFETFLW LEDEGVDVTV PDRAAADGFD YLRGRSLQWM NEQAMWGTYV
AHRNGGVPVG RIVLRDRSPE AFGALVMFFE RAVALSGMLL GVNPFDQPGV EAYKANLFAL
LGRPGYEARG EALQAEIAAL LDRR
//
