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Database: UniProt
Entry: A0A1C6VYR6_9ACTN
LinkDB: A0A1C6VYR6_9ACTN
Original site: A0A1C6VYR6_9ACTN 
ID   A0A1C6VYR6_9ACTN        Unreviewed;       546 AA.
AC   A0A1C6VYR6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN   ORFNames=GA0070603_5924 {ECO:0000313|EMBL:SCL71426.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL71426.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL71426.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL71426.1,
RC   ECO:0000313|Proteomes:UP000198605};
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; FMIB01000002; SCL71426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6VYR6; -.
DR   STRING; 47854.GA0070603_5924; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000198605; 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; 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}.
FT   DOMAIN          83..248
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   546 AA;  55268 MW;  A072F5941C858FFF CRC64;
     MSDLLAGRAD IAAGLAVHGA DAVDGSAPAS VRAALVAADL PARLAAKDPT LWGPDAEATA
     RTRLGWLDTH TRSRELLPQL AELTEELADL DHVVLAGMGG SSLAPEVLAR TLGRPLTVLD
     TTDPGQVRAA LADRLERTVV VVASKSGGTV ETDSVRRAYL QAFLDAGLTE AEAARHFVVV
     TDPGSPLESV ADEMGVVVIQ SDPEVGGRYS ALTAFGLTPA ALAGVPVADL LDDAEALAGA
     LGRDRDNPGL ALGAALGAAA TSGRATVALV SDGTGLDGLG DWVEQLLAES TGKAGRGILP
     VVVESPDAPG ATGPGVLTVG YGGALGPGVA PGPADVAVNG PLGAQFLTWE YATAVAAAVL
     DVDPFDQPDV AGSKEHTARL LAAGPPAESP SATDGAVEVY APAGAPADLA GALRWLLDGL
     GDDGYLAVSA YLDRWADAAV AGLRPLLARA TPRPVTFGWG PRYLHSTGQY HKGGPRAGSH
     LQVTGAVTDD LPVPGRPYTF GDLQAAQAAG DRRALADRGR PVLRLHLTER AAGVAQLLDA
     AGRTLT
//
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