ID A0A1J9PIQ8_9EURO Unreviewed; 749 AA.
AC A0A1J9PIQ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=ACJ73_08892 {ECO:0000313|EMBL:OJD16337.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD16337.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD16337.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD16337.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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:OJD16337.1}.
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; LGTZ01002265; OJD16337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9PIQ8; -.
DR STRING; 1658174.A0A1J9PIQ8; -.
DR VEuPathDB; FungiDB:ACJ73_08892; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000242791; Unassembled WGS sequence.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd06135; Orn; 1.
DR CDD; cd03085; PGM1; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR045244; PGM.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00929; RNase_T; 1.
DR PRINTS; PR00509; PGMPMM.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000242791}.
FT DOMAIN 1..171
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 749 AA; 81866 MW; 4A96250649D48E74 CRC64;
MTGLDPRTDK ILQICCFITD ADLNLLDHTG FEAIIHHPKS VLDNMNDWCI DTHGRSGLTA
AVAASKTTPT AAAEGLLAYI MKHVPQKRTG LLAGNSVHAD KAFLACEPYA MVLEWLHYRL
LDVSSVKEAV RRWGDEEVLR NAPKKEFLHL AREDILESIE EMRYYRRPSR LLAIWALVPT
TNATSHCVAK LLNMSVKTVS ITPFQDQKAG TSGLRKKVTV FQQPNYSESF ITSILLSIPE
GVEGSFLVIG GDGRYYNPEV VQLIAKIGAA YGVKKLLVGH NGILSTPAAS HVIRKRKATG
GILLTASHNP GGPNADFGIK YNLSNGAPAP ESVTNKIYET SKNLTSYKIA EIPDIDLAHT
GVQTCGPLEV EVIHSTTDYV DMLKEIFDFD LIKSLFKIHP DFKVLFDALH GVTGPYGKAI
FLDELGLPAS SVQNCVPSPD FGGGHPDPNL TYAHSLVEAV DKNGIQFGAA SDGDGDRNMI
YGAKTFVSPG DSLAIIAHHA KLIPYFRNQG VYGLARSMPT SGAVDLVAKA QGLQCYEVPT
GWKFFCALFD TKRMSICGEE SFGTGSNHIR EKDGLWAVIA WLNIIAGVAK ANPDKPASIA
AIQLDFWKEY GRTFFTRYDY ENVDSAGASK VIAHLTDLIA TQKEAFVGSN VSGRKVLEAG
DFSYTDLDGS VSKNQGIYVK FDDGSRIVVR LSGTGSSGAT IRLYVERHEA DEKEFGKDAQ
EYLKENIELA VQLLKLKEFI GREEPDVKT
//
