ID A0A0Q8LMK2_9MICO Unreviewed; 540 AA.
AC A0A0Q8LMK2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=ASD93_06555 {ECO:0000313|EMBL:KRB37974.1};
OS Microbacterium sp. Root180.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB37974.1, ECO:0000313|Proteomes:UP000050802};
RN [1] {ECO:0000313|EMBL:KRB37974.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB37974.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB37974.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB37974.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {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:KRB37974.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMHS01000002; KRB37974.1; -; Genomic_DNA.
DR RefSeq; WP_056120416.1; NZ_LMHS01000002.1.
DR AlphaFoldDB; A0A0Q8LMK2; -.
DR STRING; 1736483.ASD93_06555; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000050802; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW Reference proteome {ECO:0000313|Proteomes:UP000050802}.
SQ SEQUENCE 540 AA; 56396 MW; FFF903230C2DD045 CRC64;
MSFDIHLSGH VKSVVDETLP GLVSSLVASG ITAGDGTLWG PAAEDEASRR LGWVEAVSVS
RPLVPQIEAL RQQLAAKGVT RVVLAGMGGS SLAPEVIAQT AGVPLVILDS TAPGQVLAAI
DGDAQQGGLS QTVLVVSSKS GSTVETDSAK RAFEAAFRDL GIDPLERIVV VTDPGSPLDQ
AARADGYTVF NADPTVGGRY SALTAFGLVP TGLAGVDIAE LLDEADATLL EVAIDSPDNP
ALVLAAAIAG GEPRRDKLGL VTDGTHIVGL PDWIEQLVAE STGKEGTGIL PVVLLPVSPE
VENKPSDVQI VRLVDEAKKF HLFEHHTDEV LISGSLGAQL VVWEYATAIA GRMLGINPFD
QPDVESAKIA ARGLLDARPE PTEPAFSVDG VEVRVSDPEL AASGTVAGVL DALWSRLPED
GYVSIQAYVN RLELDQLPGL RELVAADSGR PTTFGWGPRF LHSTGQFHKG GPANGVFLQI
LEQTDVDLEI PGRPFTFGQL IQAQAAGDAS VLADGHGRPV VTLTLTDPRI EVLSLFEAAQ
//
