ID A0A0A8HR55_STAHY Unreviewed; 443 AA.
AC A0A0A8HR55;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=BUZ57_00740 {ECO:0000313|EMBL:RIO47566.1}, GLV83_03760
GN {ECO:0000313|EMBL:NJI30786.1};
OS Staphylococcus hyicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1284 {ECO:0000313|EMBL:RIO47566.1, ECO:0000313|Proteomes:UP000285625};
RN [1] {ECO:0000313|EMBL:RIO47566.1, ECO:0000313|Proteomes:UP000285625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 5959 {ECO:0000313|EMBL:RIO47566.1,
RC ECO:0000313|Proteomes:UP000285625};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:NJI30786.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1380 {ECO:0000313|EMBL:NJI30786.1};
RA Rhoads D., Shwani A., Adkins P., Calcutt M., Middleton J.;
RT "Whole genome comparisons of Staphylococcus agnetis isolates from cattle
RT and chickens.";
RL Submitted (NOV-2019) 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:RIO47566.1}.
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DR EMBL; WMFP01000025; NJI30786.1; -; Genomic_DNA.
DR EMBL; QXVO01000002; RIO47566.1; -; Genomic_DNA.
DR RefSeq; WP_039646536.1; NZ_WMFP01000025.1.
DR AlphaFoldDB; A0A0A8HR55; -.
DR STRING; 1284.SHYC_09460; -.
DR GeneID; 41073668; -.
DR KEGG; shu:SHYC_09460; -.
DR HOGENOM; CLU_037303_0_1_9; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000285625; Unassembled WGS sequence.
DR Proteomes; UP000606275; 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; 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 285
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 443 AA; 49222 MW; 4243AB4E97361C23 CRC64;
MTHIQLDYQK ALSFFEQHEI DQQADLVKSV HRTIHEGTGA GSDFLGWVDL PVDYDKAEFA
RIQKSAEQIK SNSDVLVVIG IGGSYLGARS AIEMLTPAFK KDKDTPEIIF AGHHLSSTYT
QELIDYLEGK DFSVNVISKS GTTTEPAVAF RLFKKLLEDK YGKAEAVKRI FATTDKEKGA
LKQLATNEGY ESFIVPDDVG GRFSVLTAVG LLPIAVAGID IEAMMSGAAS AREELSSDDV
TKNIAYQYAT IRNILYSKGY TTEMLINYEP SLQYFNEWWK QLFGESEGKD LKGIYPSSAN
FTTDLHSLGQ YVQEGRRFLF ETVLKVESPK HSITIEKDED DLDGLNYLAG KTVDDVNTKA
FEGTLLAHTD GGVPNLVVKV PQLDAFTYGY LVYFFEKAVA MSGYQLGVNP FNQPGVEAYK
QNMFALLGKP GFEDKKKELE ARL
//
