ID   F4X483_ACREC            Unreviewed;       605 AA.
AC   F4X483;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Phosphoglucomutase-2 {ECO:0000313|EMBL:EGI58751.1};
GN   ORFNames=G5I_13142 {ECO:0000313|EMBL:EGI58751.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI58751.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL888628; EGI58751.1; -; Genomic_DNA.
DR   RefSeq; XP_011065289.1; XM_011066987.1.
DR   RefSeq; XP_011065290.1; XM_011066988.1.
DR   RefSeq; XP_011065291.1; XM_011066989.1.
DR   AlphaFoldDB; F4X483; -.
DR   STRING; 103372.F4X483; -.
DR   EnsemblMetazoa; XM_011066987.1; XP_011065289.1; LOC105152606.
DR   EnsemblMetazoa; XM_011066988.1; XP_011065290.1; LOC105152606.
DR   EnsemblMetazoa; XM_011066989.1; XP_011065291.1; LOC105152606.
DR   GeneID; 105152606; -.
DR   KEGG; aec:105152606; -.
DR   eggNOG; KOG1220; Eukaryota.
DR   InParanoid; F4X483; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05799; PGM2; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
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   Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT   DOMAIN          53..191
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          221..325
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          337..463
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   605 AA;  68200 MW;  3C52F4A40CB02ABA CRC64;
     MTLCSMNTGD SNLDNKITEW LQWNKNPKAK DEILEYLDKG QIKVLSKLFL KRLEFGTAGL
     RGRMGPGYNQ MNDLVIVQTG QGLSKYLMDT IFDVIQKGVV IGYDGRYNSK RFAELTAAIF
     IAKNIKVYLF SQVCPTPFIP YTILKYKCAA GIMVTASHNP KDDNGYKVYW ENGAQIISPH
     DKKIQSYILN NLKPLESSWD ISQIYESSYY KDPRDDIMLH YYQDLKDNVL YPEVNRNTTL
     KFTYTAMHGV GQEYMIAAFE AANFKPFITV EEQKLPDPEF STVKFPNPEE GKSALDLSIK
     TANKNDSSII IANDPDADRL ACATKTESGE WHVFSGNELG ALLGWWMIHT YQVIHPDVDL
     SKTYMLASTV SSKILASMGK KEGFNFEETL TGFKWMGNKA IELVKDNKDV LFAYEEAIGF
     MCGSKVLDKD GISAGVRVAE LAAYLETIGL TLSDKLEEIY EEYGHHINDN SYWICHDPDT
     IKTIFERLRN YSGKSDAYPT GILKGKYIIT GIRDLTTGYD NTKPDNKAIL PVSKSSQMIT
     FTFKNGLVTT LRTSGTEPKI KYYNELCGSP GEDLNKLKCI LSEMVSAIVA EFLQPEVNGL
     IAREE
//