AGM1_CANAX
ID AGM1_CANAX Reviewed; 544 AA.
AC Q9P4V2; Q9P8H8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000303|PubMed:11004509};
DE Short=PAGM;
DE EC=5.4.2.3 {ECO:0000269|PubMed:11004509};
DE AltName: Full=Acetylglucosamine phosphomutase;
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000303|Ref.2};
GN Name=AGM1 {ECO:0000303|PubMed:11004509};
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060 / 2024;
RX PubMed=11004509; DOI=10.1016/s0167-4781(00)00120-2;
RA Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.;
RT "Functional cloning and mutational analysis of the human cDNA for
RT phosphoacetylglucosamine mutase: identification of the amino acid residues
RT essential for the catalysis.";
RL Biochim. Biophys. Acta 1492:369-376(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Spettel C., Eschrich D., Koetter P., Entian K.;
RT "Identification and isolation of Candida albicans AGM1.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ZINC.
RX PubMed=16651269; DOI=10.1074/jbc.m600801200;
RA Nishitani Y., Maruyama D., Nonaka T., Kita A., Fukami T.A., Mio T.,
RA Yamada-Okabe H., Yamada-Okabe T., Miki K.;
RT "Crystal structures of N-acetylglucosamine-phosphate mutase, a member of
RT the alpha-D-phosphohexomutase superfamily, and its substrate and product
RT complexes.";
RL J. Biol. Chem. 281:19740-19747(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:0000269|PubMed:11004509}.
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:0000269|PubMed:11004509};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16651269};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305|PubMed:16651269};
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:0000305|PubMed:11004509}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AB032082; BAB00614.1; -; Genomic_DNA.
DR EMBL; AF253056; AAF64520.1; -; Genomic_DNA.
DR PDB; 2DKA; X-ray; 1.93 A; A/B=1-544.
DR PDB; 2DKC; X-ray; 2.20 A; A/B=1-544.
DR PDB; 2DKD; X-ray; 2.10 A; A/B=1-544.
DR PDBsum; 2DKA; -.
DR PDBsum; 2DKC; -.
DR PDBsum; 2DKD; -.
DR AlphaFoldDB; Q9P4V2; -.
DR SMR; Q9P4V2; -.
DR VEuPathDB; FungiDB:C1_13760W_A; -.
DR VEuPathDB; FungiDB:CAWG_00076; -.
DR BRENDA; 5.4.2.3; 1096.
DR UniPathway; UPA00113; UER00530.
DR EvolutionaryTrace; Q9P4V2; -.
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; 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; PF00408; PGM_PMM_IV; 1.
DR PIRSF; PIRSF016408; PAGM; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT CHAIN 1..544
FT /note="Phosphoacetylglucosamine mutase"
FT /id="PRO_0000148016"
FT ACT_SITE 66
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000305|PubMed:16651269"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000305|PubMed:16651269"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:16651269"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:16651269"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:16651269"
FT BINDING 387..389
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16651269"
FT BINDING 512..516
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16651269"
FT BINDING 521
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16651269"
FT CONFLICT 238
FT /note="K -> R (in Ref. 2; AAF64520)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="K -> N (in Ref. 2; AAF64520)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="S -> Y (in Ref. 2; AAF64520)"
FT /evidence="ECO:0000305"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 37..53
FT /evidence="ECO:0007829|PDB:2DKA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:2DKA"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2DKA"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2DKD"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 312..327
FT /evidence="ECO:0007829|PDB:2DKA"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 435..448
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 453..457
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:2DKD"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2DKD"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:2DKD"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:2DKA"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:2DKA"
FT HELIX 529..543
FT /evidence="ECO:0007829|PDB:2DKA"
SQ SEQUENCE 544 AA; 60478 MW; B022662342FA6D58 CRC64;
MSIEQTLSQY LPSHPKPQGV TFTYGTAGFR MKADKLDYVT FTVGIIASLR SKYLQGKTVG
VMITASHNPP EDNGVKVVDP LGSMLESSWE KYATDLANAS PSPSNDSEGE KNSLVEVIKN
LVSDLKIDLS IPANVVIARD SRESSPALSM ATIDGFQSVP NTKYQDFGLF TTPELHYVTR
TLNDPDFGKP TEDGYYSKLA KSFQEIYTIC ESNNEKIDIT IDAANGVGAP KIQELLEKYL
HKEISFTVVN GDYKQPNLLN FDCGADYVKT NQKLPKNVKP VNNKLYASFD GDADRLICYY
QNNDNKFKLL DGDKLSTLFA LFLQQLFKQI DPTKISLNIG VVQTAYANGS STKYVEDVLK
IPVRCTPTGV KHLHHEAENF DIGVYFEANG HGTVIFNPEA EKKIFDYKPN NDNEAKAIKV
LQNFSQLINQ TVGDAISDLL AVLIVVHYLK LSPSDWDNEY TDLPNKLVKV IVPDRSIFKT
TNAERTLVEP KGMQDEIDKL VAQYPNGRSF VRASGTEDAV RVYAEADTQN NVEELSKAVS
ELVK
