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Database: UniProt
Entry: Q54TE6_DICDI
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ID   Q54TE6_DICDI            Unreviewed;       469 AA.
AC   Q54TE6;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Phosphoglucosamine mutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DDB_G0281789 {ECO:0000313|EMBL:EAL66656.1};
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL66656.1, ECO:0000313|Proteomes:UP000002195};
RN   [1] {ECO:0000313|EMBL:EAL66656.1, ECO:0000313|Proteomes:UP000002195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000313|EMBL:EAL66656.1,
RC   ECO:0000313|Proteomes:UP000002195};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RG   The Dictyostelium discoideum Sequencing Consortium;
RA   Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA   White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA   Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA   Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA   Noegel A.A., Barrell B., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL66656.1}.
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DR   EMBL; AAFI02000042; EAL66656.1; -; Genomic_DNA.
DR   RefSeq; XP_640645.1; XM_635553.1.
DR   AlphaFoldDB; Q54TE6; -.
DR   SMR; Q54TE6; -.
DR   STRING; 44689.Q54TE6; -.
DR   PaxDb; 44689-DDB0204675; -.
DR   GeneID; 8623256; -.
DR   KEGG; ddi:DDB_G0281789; -.
DR   dictyBase; DDB_G0281789; -.
DR   eggNOG; KOG1220; Eukaryota.
DR   HOGENOM; CLU_016950_7_1_1; -.
DR   InParanoid; Q54TE6; -.
DR   OMA; QSGHVIF; -.
DR   PhylomeDB; Q54TE6; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central.
DR   GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR   CDD; cd05803; PGM_like4; 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; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR024086; GlmM_arc-type.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002195}.
FT   DOMAIN          9..133
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          174..264
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          274..375
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          417..464
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   469 AA;  51486 MW;  CCB7099F09B2AFC8 CRC64;
     MSHMIRSISG VRGVVGADQS WTPTLVANHI IAFTQLLESS HYNQNQKKIV VGRDSRVSGP
     WFEMITNGSL ISRGYQVIHI DIASTPTVQY MVEKTKSSGG IVITSSHNPI EWNGLKFIGP
     DGLFIAPKEC EILFSMADKP EEFKFSGYDQ LGKIEKCVDA NQQHVGAILS LAFLDISKIR
     ERRFKVCLDS VNGAGGPIMS YLLTQLNCEV IGINLETTGL FAHTPEPVPS NLGQLCEMVV
     KYKADFGIAV DPDVDRCVFI DEHGKPLGEE YTLAMAVELV LGDCGRRGNV CKNLSSSRAI
     DDICKKYESQ VICAPVGEIQ VAKKMQQVNA VIGGEGNGGV MLPDIHIGRD APVAATLALQ
     LMANRYSQAP SISKLKETLP TYEIVKLKAG IEGLDPDSIL AEYTSQFINK PGVVINQEDG
     LKIDSQDWWV HLRKSNTEHI IRVIAEAKSV KEATDIATKF IQEIESKRK
//
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