ID A0A1C5J167_9ACTN Unreviewed; 549 AA.
AC A0A1C5J167;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=GA0070613_3818 {ECO:0000313|EMBL:SCG64265.1};
OS Micromonospora inositola.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG64265.1, ECO:0000313|Proteomes:UP000198221};
RN [1] {ECO:0000313|EMBL:SCG64265.1, ECO:0000313|Proteomes:UP000198221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG64265.1,
RC ECO:0000313|Proteomes:UP000198221};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT607754; SCG64265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5J167; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000198221; Chromosome i.
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; IPR001347; SIS_dom.
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.
DR PROSITE; PS51464; SIS; 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:UP000198221}.
FT DOMAIN 83..230
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 549 AA; 55931 MW; 16AFE2F6F0802DB7 CRC64;
MSDLLAGPAD AAAGLAVYGA DAVDRSAPAS ARDALVTRGV PAALAAKDPT LWGPEAEATA
KARLGWLDTH LRSRELLPQL AELTAELEDL DHVVLAGMGG SSLAPEVIAR TLGRPLTVLD
STDPGQVRAA LADPLERTVV VISSKSGSTV ETDSHRRVYW QAFLDAGMTE AEAARHFVVV
TDPGSPLAET AAEMGVVTIF ADPEVGGRYS ALTAFGLVPA ALAGAEVTEL LDEAEALSGS
LGRDRDNPGL ALGAALAAAA TTGRDKVALV GDGTGIDGLG DWAEQLLAES TGKAGVGILP
VVVESPRAPG TAGPDVLTVS YGGALTAGDV PGGGGSPDVA VNGPLGAHFL TWEYAIAIAG
VVLGVDPFDQ PNVTESKENT ARILASAPPA ETPSFVEGAV EVYAPAAAPG DLAGVLRWLL
DGLGDDGYLA VLAYLDRQAD AAVAGLRPLL AEAAGRPVTF GWGPRFLHST GQYHKGGPQV
GSFLQVTGAV TEDLPVPGRP YTFGELQAAQ AAGDRQALAG RERPVLRLHL TERAAGVAQL
LDAAGRTRT
//
