ID   AGM1_ENCCU              Reviewed;         530 AA.
AC   Q8SSL7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable phosphoacetylglucosamine mutase {ECO:0000250|UniProtKB:P38628};
DE            Short=PAGM;
DE            EC=5.4.2.3 {ECO:0000250|UniProtKB:P38628};
DE   AltName: Full=Acetylglucosamine phosphomutase {ECO:0000250|UniProtKB:P38628};
DE   AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000250|UniProtKB:P38628};
GN   Name=PCM1 {ECO:0000250|UniProtKB:P38628}; OrderedLocusNames=ECU01_0650;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11157783; DOI=10.1101/gr.164301;
RA   Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA   Weissenbach J., Saurin W., Vivares C.P.;
RT   "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT   parasite Encephalitozoon cuniculi (Microspora).";
RL   Genome Res. 11:198-207(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC       the synthesis of uridine diphosphate/UDP-GlcNAc, which is a
CC       biosynthetic precursor of chitin and also supplies the amino sugars for
CC       N-linked oligosaccharides of glycoproteins.
CC       {ECO:0000250|UniProtKB:P38628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-
CC         glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513,
CC         ChEBI:CHEBI:57776; EC=5.4.2.3;
CC         Evidence={ECO:0000250|UniProtKB:P38628};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9P4V2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC       alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC       {ECO:0000250|UniProtKB:P38628}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; AL391737; CAD24935.1; -; Genomic_DNA.
DR   RefSeq; XP_965900.1; XM_960807.1.
DR   AlphaFoldDB; Q8SSL7; -.
DR   SMR; Q8SSL7; -.
DR   STRING; 284813.Q8SSL7; -.
DR   PRIDE; Q8SSL7; -.
DR   GeneID; 860240; -.
DR   KEGG; ecu:ECU01_0650; -.
DR   VEuPathDB; MicrosporidiaDB:ECU01_0650; -.
DR   HOGENOM; CLU_022890_1_0_1; -.
DR   InParanoid; Q8SSL7; -.
DR   OMA; WEAYATK; -.
DR   OrthoDB; 345441at2759; -.
DR   UniPathway; UPA00113; UER00530.
DR   Proteomes; UP000000819; Chromosome I.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03086; PGM3; 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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR016657; PAGM.
DR   Pfam; PF02878; PGM_PMM_I; 2.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PIRSF; PIRSF016408; PAGM; 1.
DR   SUPFAM; SSF53738; SSF53738; 4.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Isomerase;
KW   Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..530
FT                   /note="Probable phosphoacetylglucosamine mutase"
FT                   /id="PRO_0000381747"
FT   ACT_SITE        62
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         278
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         369..371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         481..485
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT   BINDING         490
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4V2"
SQ   SEQUENCE   530 AA;  58611 MW;  E74F296E1F93C1B6 CRC64;
     MDNALIADEN LKKPSKPAYY GTAGYRSKTS DLNNILCRAS LIAYLRSTTF AGKIIGVMIT
     ASHNPVEYNG IKIIDHNGDM LDEVWEEYSD RIVNCDDEKL AREMKKILRS CSNQSELGEG
     VRGHVVLGRD TRDSGERLCN NIRSVLGKLN CTVDDYGVVT TPELHFLVRK CNTENRVVDK
     AEYMKNIAHN FNSLSSITKG NLRMMIDTAN GVADMKLKEL DGMLDGKLNY EVLNDPKGIL
     NLDCGADFVK TKKRAPRLEA LSSSGFSQAA NRICASFDGD VDRLIFFTGP KDTEIFDGDS
     QAVFLALYIR SLLDRIESRL SIGVVLSYYS NNAAVDVLPP ESFKVVMAQT GVKNFVSAAR
     EFDVGIYFEP NGHGSVCFSQ ACIDEIEKGS TKSHAILKIL ANLFDPCIGD ALANFVIFKA
     LMGSADDLRK FRENPSRLLT VKIVDKNSIK VDQKNQVIEP KELQDKIDVE ALSLGGRSFV
     RPSGTEDVVR VYAECPSEAD ADLLCLKVAQ HVYDMCNGIG DHPEIDYTSK