PGM_ASPOR
ID PGM_ASPOR Reviewed; 555 AA.
AC P57749; Q2UKM8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphoglucomutase {ECO:0000250|UniProtKB:P37012};
DE Short=PGM {ECO:0000250|UniProtKB:P37012};
DE EC=5.4.2.2 {ECO:0000250|UniProtKB:P37012};
DE AltName: Full=Glucose phosphomutase;
GN Name=pgmA; ORFNames=AO090003000746;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.;
RT "Molecular cloning and characterization of phosphoglucomutase from
RT Aspergillus oryzae.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Catalyzes the reversible interconversion of glucose 1-
CC phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The
CC reverse reaction is an essential step for biosynthesis because glucose
CC 1-phosphate is the starting point for the synthesis of UDP-glucose,
CC which acts as a precursor for the synthesis of oligosaccharides and
CC trehalose. {ECO:0000250|UniProtKB:P37012}.
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:0000250|UniProtKB:P37012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P37012};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P37012};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P37012}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AB032275; BAB12235.1; -; mRNA.
DR EMBL; AP007155; BAE57887.1; -; Genomic_DNA.
DR RefSeq; XP_001819889.1; XM_001819837.2.
DR AlphaFoldDB; P57749; -.
DR SMR; P57749; -.
DR STRING; 510516.P57749; -.
DR PRIDE; P57749; -.
DR EnsemblFungi; BAE57887; BAE57887; AO090003000746.
DR GeneID; 5991872; -.
DR KEGG; aor:AO090003000746; -.
DR VEuPathDB; FungiDB:AO090003000746; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR OMA; DIYKIYA; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573; PTHR22573; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..555
FT /note="Phosphoglucomutase"
FT /id="PRO_0000147793"
FT ACT_SITE 114
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 555 AA; 60357 MW; 6AA1DB84878C6DF1 CRC64;
MSIQTVSFQS FTDQKPGTSG LRKKVKVFQQ PNYSESFITS ILLSIPEGAK DAFLVIGGDG
RYYNPEAIQK IAKISAAYGV KKLLVGQNGI LSTPAASNLI RVRKATGGIL LTASHNPGGP
NADFGIKYNL SNGAPAPETV TNKIYETSKT LTSYNYAEIP ELDLSSIGSK TYGPLEVEVV
HSTSDYVKMM KEIFDFDLIK EFLNTHKDFK VLFDGMHGVT GPYGVDIFVN ELGLPSSSTM
NCVPSPDFNG GHPDPNLVYA HELVEAVDKN GIHFGAASDG DGDRNMIYGA NTFVSPGDSL
AIISHHAKLI PYFQKQGVYG LARSMPTSGA VDLVAKAQGL QSYEVPTGWK FFCNLFDNKK
ISICGEESFG TGSNHIREKD GLWAIVAWLN IIAGVAKEKP DQTPSIASIQ NDFWQAYGRT
FFTRYDYENV DSDGANKVIA ILSDKVANKD SFVGSTVSGR KVTDVGNFSY TDLDGSVSKN
QGLYAKFDDG SRIIVRLSGT GSSGATIRLY IEKYESDKSK FGLTASEYLK DNVALALSLL
NFKEFIGREE PDVRT
