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Database: UniProt
Entry: C1MKX8_MICPC
LinkDB: C1MKX8_MICPC
Original site: C1MKX8_MICPC 
ID   C1MKX8_MICPC            Unreviewed;       600 AA.
AC   C1MKX8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   Name=PGM1 {ECO:0000313|EMBL:EEH59450.1};
GN   ORFNames=MICPUCDRAFT_70805 {ECO:0000313|EMBL:EEH59450.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH59450.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH59450.1,
RC   ECO:0000313|Proteomes:UP000001876};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; GG663736; EEH59450.1; -; Genomic_DNA.
DR   RefSeq; XP_003056074.1; XM_003056028.1.
DR   AlphaFoldDB; C1MKX8; -.
DR   STRING; 564608.C1MKX8; -.
DR   GeneID; 9681988; -.
DR   KEGG; mpp:MICPUCDRAFT_70805; -.
DR   eggNOG; KOG0625; Eukaryota.
DR   OMA; YIPDYAG; -.
DR   OrthoDB; 5476118at2759; -.
DR   Proteomes; UP000001876; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03085; PGM1; 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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR045244; PGM.
DR   PANTHER; PTHR22573:SF59; PHOSPHOGLUCOMUTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001876}.
FT   DOMAIN          55..192
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          227..330
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          341..442
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   600 AA;  64793 MW;  936A0D00C8478990 CRC64;
     MVASCAQPSA TLRGQFSVKS YFKSSRATTR RMSVQIISSA GNKVSDVPTT PIDGQKTGTS
     GLRKKASVFA SENYLANWVQ SLFLALPREE VVGSAMVLGG DGRWFNKEAA QIIIKLAAGN
     GVKKMFVGQN GFLATPAASA VIRARKANGG FIMSASHNPG GPKEDWGIKF NYSSGEPAPE
     KITDKIYGFT QTVDVLKMAD IPEIDLSVCG TTKFNDFEVE VIDPVADYLA LVSEVFDMEL
     IKSLLTRSDF TMKFDAMHAI TGAYAKPIFV EALGADPSSC VNDTPKEDFG GGHPDPNLTY
     AEELVKIMYA NDAPDFGAAS DGDGDRNMIL GNNFFVTPSD SVAIIAANAQ DCIPYFEGRG
     GLKGLARSMP TAAALDRVAA ALGVECFETP TGWKFFGNLM DAGRLSICGE ESFGTGSDHI
     REKDGPWAVL AWLSILAHRN KEIPVGGSKV TVEQITKEHW AKYGRNFFSR YDYEGCEAGP
     CNEMVEYLRS VAASAKQGDT FGSYELDFAD DFEYTDPIDG SVSSNQGVRF VFTDGSRFIF
     RLSGTGSSGA TVRMYIEQYE PDVTKQNIDA QDALAPLINV ALDTSKLKEF TGRDSPTVIT
//
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