ID A0A067P386_PLEOS Unreviewed; 862 AA.
AC A0A067P386;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00012731};
DE EC=5.4.2.3 {ECO:0000256|ARBA:ARBA00012731};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000256|ARBA:ARBA00032065};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|ARBA:ARBA00031926};
GN ORFNames=PLEOSDRAFT_1092332 {ECO:0000313|EMBL:KDQ30842.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ30842.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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:0000256|ARBA:ARBA00000558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:0000256|ARBA:ARBA00004865}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; KL198006; KDQ30842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067P386; -.
DR STRING; 1137138.A0A067P386; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1092332; -.
DR HOGENOM; CLU_013180_0_0_1; -.
DR InParanoid; A0A067P386; -.
DR OrthoDB; 1475at2759; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000027073; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03086; PGM3; 1.
DR CDD; cd01908; YafJ; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR049023; AMG1_II.
DR InterPro; IPR049022; AMG1_III.
DR InterPro; IPR026869; EgtC-like.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016657; PAGM.
DR PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR Pfam; PF21405; AMG1_II; 1.
DR Pfam; PF21404; AMG1_III; 1.
DR Pfam; PF13230; GATase_4; 1.
DR Pfam; PF02878; PGM_PMM_I; 2.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073}.
FT DOMAIN 538..847
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 862 AA; 93874 MW; 7E0E53E4EF049CC3 CRC64;
MSGLPVASIK ELSEKHPKPS DIKFTYGTAG FRTLASVLDS VLFRVGILAG LRSKKLDGKT
IGVMVTASHN PEQDNGVKLV DPRGEMLESS WESHATTLSN ASSTDEFISA LEAFVRDAKI
DLSKPARVVY AMDTRPSGPA LVSALEDGLR AIGADGRNAG VTTTPILHYL VRAINTKGTA
EAYGDDSEDG YYTKLTNAFK KLVSAKPTPS PLLIDCANGV GANAAKKLAE YLGDTFSLVL
ENTSITAPGA LNNACGADFV KTTQKLPSSL SNIIKPGQRG CSLDGDADRL MYFHLDDRGQ
FRMLDGDKIA ALVAAFIVEL VKAAGLDESI KVGVVQTAYA NGASTKYLAE RLPVKCVSTG
VKHLHHAAEH YDVGVYFEAN GHGTVLFSPD TLAKLADYQP STPAQSTAVE HLVNLTQLIN
QTVGDALSDM LLVEVVLAHK AYGGLEWDSL YVDLPNRLVK VVVADRHIFK TVDAERRLTS
PVGLQDKIDS LVGKYEGGRS FVRPSGTEDV VRVYAEAVVK SQADELAFRV AGLHFEMCRF
VIYKGTSPVQ LSHLLTRPCH SIINQAFDSR LRLDRRRPIN GDGFGVGWYD PNYDPELGTQ
PCIFTSVTPA WNNINLTRLA EKIKSPLVFA HVRATTAGSL SLDNCHPFQY GKLMFMHNGA
IAEWSRVKRK VQNCLPDCAY DNVHGNTDSE MAFALFLSML PNPDANTFTP HELQKAMLDT
IAALNAFAKE AGVTEPSLMN FCITDGESVV ATRYISSRTD EAASLWYSSG TTFSEYAAGG
KYKMSKADKR ENIIMIASEP LTFEKADWME IRTNHMVVIT PKFNLLQIPI RDEFYVPPSD
PAALTRDTDF AYGKGLLSVS RS
//
