ID U3JJ60_FICAL Unreviewed; 572 AA.
AC U3JJ60;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000256|ARBA:ARBA00012731, ECO:0000256|PIRNR:PIRNR016408};
DE Short=PAGM {ECO:0000256|PIRNR:PIRNR016408};
DE EC=5.4.2.3 {ECO:0000256|ARBA:ARBA00012731, ECO:0000256|PIRNR:PIRNR016408};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000256|ARBA:ARBA00032065, ECO:0000256|PIRNR:PIRNR016408};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|ARBA:ARBA00031926, ECO:0000256|PIRNR:PIRNR016408};
GN Name=PGM3 {ECO:0000313|Ensembl:ENSFALP00000002814.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002814.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002814.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002814.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide
CC critical to multiple glycosylation pathways including protein N- and O-
CC glycosylation. {ECO:0000256|PIRNR:PIRNR016408}.
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 ECO:0000256|PIRNR:PIRNR016408};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR016408,
CC ECO:0000256|PIRSR:PIRSR016408-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR016408,
CC ECO:0000256|PIRSR:PIRSR016408-3};
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, ECO:0000256|PIRNR:PIRNR016408}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|PIRNR:PIRNR016408}.
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DR AlphaFoldDB; U3JJ60; -.
DR STRING; 59894.ENSFALP00000002814; -.
DR Ensembl; ENSFALT00000002826.2; ENSFALP00000002814.2; ENSFALG00000002701.2.
DR eggNOG; KOG2537; Eukaryota.
DR GeneTree; ENSGT00390000000509; -.
DR HOGENOM; CLU_022890_1_0_1; -.
DR OrthoDB; 1475at2759; -.
DR UniPathway; UPA00113; UER00530.
DR Proteomes; UP000016665; Chromosome 3.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03086; PGM3; 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 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; 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; PF02878; PGM_PMM_I; 2.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PIRSF; PIRSF016408; PAGM; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR016408};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR016408};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016408};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 52..100
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 102..167
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 178..283
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21405"
FT DOMAIN 297..433
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 450..525
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT COILED 386..413
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 64
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT BINDING 368..370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 495..499
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ SEQUENCE 572 AA; 63586 MW; 7578046FF3EBBDD4 CRC64;
MDLEALRRYS ALHPKPAGLT LQYGTAGFRS RAEQLDHIVF RMGLLAILRS KAVTATIGIM
VTASHNPEED NGVKLVDPLG EMLHPSWEEY ATQLANAEEQ ELQKVITEIC QKAEVNLHKD
ASVFIGRDTR PSSKKLSQSV IDGIQVLGGQ YHDYGLVTTP QLHYMVCCQN TQGQYGKATL
EGYYEKLSKA FMELIKQSHC SGENQKHLKI DCANGIGALK LSEMKPYFPQ EVVIHIYNDG
TKEKLNHLCG ADFVKVQQKP PGGLDMKPNE RCCSFDGDAD RIVYYYKDTA GHFHLIDGDK
IATLISIFLK ELLVKQDFKM AVVQTAYANG NSTRYLQETL KVPVHCVKTG VKHLHHKAQE
FDVGVYFEAN GHGTVLFSKT AETKIRQLVK EEKDDEKREA AKMLENMIDL INQTVGDAVS
DMLVIEAILA LKGLTVQQWD ALYTDLPNRL LKVQVADRRV IDTTDAERRA LTPPGLQEKI
DALVKKYKLS RAFVRPSGTE DVVRIYAEAD TQENADALAH EVSLAVFHLA GGKGAPPQRN
SAPPLVHFHI VPEIQVPHPQ STGHGCMTGA LL
//
