ID A0A0Q4VDC2_9MICO Unreviewed; 532 AA.
AC A0A0Q4VDC2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=ASF23_00905 {ECO:0000313|EMBL:KQO64790.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO64790.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO64790.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO64790.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO64790.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO64790.1};
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:KQO64790.1}.
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DR EMBL; LMMJ01000001; KQO64790.1; -; Genomic_DNA.
DR RefSeq; WP_055947668.1; NZ_LMMJ01000001.1.
DR AlphaFoldDB; A0A0Q4VDC2; -.
DR STRING; 1736311.ASF23_00905; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000050821; 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:UP000050821}.
SQ SEQUENCE 532 AA; 54629 MW; 2443987FBDB84F7E CRC64;
MTVSIAASGD AAVAVDSVVP QLVSDYVASG ITAQEPDLWG PAAESEAAVR LGWVEAVATS
RPLVAEITKL RKHLRHRGVD HVVLAGMGGS SLAPEVIAGT YGVDLVVLDS TDPAQVAAAV
GAELDRTVLV VSSKSGSTLE TDSQRRVYEA AFRAAGIDPA ERIVVVTDPG SALEQTARDA
GYTVFLADPT VGGRYSALTA FGLVPSGLAG ADIAELLDEA EAISPLLATD SDENPGLVLG
AVLGGTEPLR DKIAIVADGT HIRGFGDWIE QLIAESTGKL GRGLLPVVLD VDSPELTADL
HDVQVIRLVG SREDEREVVD GEVEISGSLG GQIMVWEYAV VVAGRLLGIN PFDQPDVEAA
KVAARALLEA TPAPVAAAFE QDGIAVHATG DVTTGTTLTE ALSGLLDHVG PDGYVAIQAY
VDRGAPTGIP GLRDLVAART GRPVTFGFGP RFLHSTGQYH KGGPASGVFL QIVASDSADL
EIPGRPFTFG QLIRAQAAGD AGVLADHGRP VLTLTVSDVG AATLAIAGAL RS
//
