ID L2GX91_VAVCU Unreviewed; 542 AA.
AC L2GX91;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VCUG_00137 {ECO:0000313|EMBL:ELA48301.1};
OS Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Vavraia.
OX NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA48301.1, ECO:0000313|Proteomes:UP000011081};
RN [1] {ECO:0000313|Proteomes:UP000011081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vavraia culicis strain floridensis.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; GL877405; ELA48301.1; -; Genomic_DNA.
DR RefSeq; XP_008073161.1; XM_008074970.1.
DR AlphaFoldDB; L2GX91; -.
DR STRING; 948595.L2GX91; -.
DR GeneID; 19878028; -.
DR VEuPathDB; MicrosporidiaDB:VCUG_00137; -.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; L2GX91; -.
DR OMA; WEAYATK; -.
DR OrthoDB; 1475at2759; -.
DR Proteomes; UP000011081; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR049022; AMG1_III.
DR PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR Pfam; PF21404; AMG1_III; 1.
DR Pfam; PF02878; PGM_PMM_I; 2.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
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:UP000011081}.
FT DOMAIN 57..99
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 123..171
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 326..404
FT /note="Phosphoacetylglucosamine mutase AMG1"
FT /evidence="ECO:0000259|Pfam:PF21404"
FT DOMAIN 488..515
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 237..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60872 MW; B3CA5BD740FFF945 CRC64;
MDIKSLLTKN LPSTLKKPSS TLHYGTSGYR DIPSKLPISR TTLCAYMRSS TLAGKYIGIL
LTASHNHARD NGIKLVDHNG EMFDHTWETI VNKIVNCEDN TFYSELNKVH RNYGNFRQFG
DGPKANIMVG RDTRESGVKL VEEIVELMGN FNCSVVDYGV VSTPQLHYLV ACSNKLNMLV
EKERYFDMFV DFIRFADLRE KVKVDTSNGV AGYVLSGINE RLCAVGYFDD GKETGSENTA
KQFDDEKEHG SANACEKEHG TDMKQELFVI TNKDGEVNDR CGAQYIQYEK EVPCHLENAK
GLYASFDGDM DRFIYFTVND GLTYMDGDRQ ASILVRYLSE KVNCRIGCVL SDYSNSAAVN
YVGKYCEAVR VRTGIKNFIK KSKEYDIGVY NEPNGHGGIF FGKEDIGDEE INKIIEMYRD
CVADPLANFL LLEYLRKTRP ALFEDTYVPF PSRMLQVSVA DPTVVVNSEN LDVLEPVALK
NVIGNIMKNE KGKVFVRPSG TENVIRIFCE AKDNVDVMCL TVAQAVYDIC GGVGKHPEIS
YV
//
