PGM_EMENI
ID PGM_EMENI Reviewed; 556 AA.
AC Q9P931; C8VJB7; Q5B9B3;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=pgmB; ORFNames=AN2867;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=10660061; DOI=10.1007/pl00008643;
RA Hoffmann B., LaPaglia S.K., Kubler E., Andermann M., Eckert S.E.,
RA Braus G.H.;
RT "Developmental and metabolic regulation of the phosphoglucomutase-encoding
RT gene, pgmB, of Aspergillus nidulans.";
RL Mol. Gen. Genet. 262:1001-1011(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalyzes the reversible interconversion of glucose 1-
CC phosphate and glucose 6-phosphate (PubMed:10660061). Key enzyme in
CC hexose metabolism. The reverse reaction is an essential step for
CC biosynthesis because glucose 1-phosphate is the starting point for the
CC synthesis of UDP-glucose, which acts as a precursor for the synthesis
CC of oligosaccharides and trehalose (By similarity).
CC {ECO:0000250|UniProtKB:P37012, ECO:0000269|PubMed:10660061}.
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; AF135264; AAF36531.1; -; Genomic_DNA.
DR EMBL; AACD01000051; EAA63438.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83845.1; -; Genomic_DNA.
DR RefSeq; XP_660471.1; XM_655379.1.
DR AlphaFoldDB; Q9P931; -.
DR SMR; Q9P931; -.
DR STRING; 162425.CADANIAP00010223; -.
DR PRIDE; Q9P931; -.
DR EnsemblFungi; CBF83845; CBF83845; ANIA_02867.
DR EnsemblFungi; EAA63438; EAA63438; AN2867.2.
DR GeneID; 2874032; -.
DR KEGG; ani:AN2867.2; -.
DR VEuPathDB; FungiDB:AN2867; -.
DR eggNOG; KOG0625; Eukaryota.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; Q9P931; -.
DR OMA; DIYKIYA; -.
DR OrthoDB; 555015at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:AspGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..556
FT /note="Phosphoglucomutase"
FT /id="PRO_0000147794"
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"
FT CONFLICT 447..459
FT /note="VDNKSSFVGSTIS -> ESTTRAHLLAAPSL (in Ref. 1;
FT AAF36531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 60684 MW; EDFB1C08219E0775 CRC64;
MSVQTVSIQP FGDQKPGTSG LRKKVKIFQQ ENYTESFLTS IFLSIPEGAQ DAFLVIGGDG
RYYNSDVIQK IAKIGAAYGV KKLIVGQNGI LSTPAASNLI RKRKATGGIL LTASHNPGGP
DNDFGIKYNL TNGAPAPEQV TNKIYEVSKS LTSYKYIDLP EVDTTTVGTR SYGPLEVEVV
HSTEDYVSMM KEIFDFDLIR SFLKKHPDFK VLFDGMHGVT GPYGIDIFVN ELGLPSSSTM
NCIPKPDFGG GHPDPNLVYA HELVEAVDKN GIHFGAASDG DGDRNMIYGA NTFVSPGDSL
AIIAHHAKLI PWFQKHGVDG LARSMPTSGA VDRVAKAQGL QSYEVPTGWK FFCNLFDNKK
MSICGEESFG TGSNHIREKD GVWAIVAWLN VIAGVAEQKP NETPSIASIQ AEFWETYGRT
FFTRYDYENV DSDGANKLIA ALSEKAVDNK SSFVGSTISG RKVVDSGNFA YTDLDGSVTK
NQGLYVKFDD GSRLVVRLSG TGSSGATIRL YVEKYEGDKS KYQMATQDYL KDNVGLALEL
LKFKEFVGRE EPDVKT
