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Database: UniProt
Entry: C0KJJ8_LOCMI
LinkDB: C0KJJ8_LOCMI
Original site: C0KJJ8_LOCMI 
ID   C0KJJ8_LOCMI            Unreviewed;       560 AA.
AC   C0KJJ8;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 36.
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};
OS   Locusta migratoria (Migratory locust).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Oedipodinae; Locusta.
OX   NCBI_TaxID=7004 {ECO:0000313|EMBL:ACM78949.1};
RN   [1] {ECO:0000313|EMBL:ACM78949.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tang B., Wang S.G., Zhang F., Zhang W.Q.;
RT   "Characterization and expression patterns of a phosphoglucomutase from
RT   Locusta migratoria.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- 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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; FJ609649; ACM78949.1; -; mRNA.
DR   AlphaFoldDB; C0KJJ8; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF2; PHOSPHOGLUCOMUTASE; 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   2: Evidence at transcript level;
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT   DOMAIN          16..155
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          205..297
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          308..420
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   560 AA;  60686 MW;  7DFDD9CFE138E935 CRC64;
     MSLNVENVKT NAFGDQKPGT SGLRKAVKVF QQPNYTENFV QSILSSLGDK LQGSTLIVGG
     DGRFYCKEAV DKIIKICAAN KVSKLFVGQN GILSTPAVSA LIRTHKATGA IILTASHNPG
     GPDKDFGIKF NVSNGGPAPD GVTNAIFELS KTLSSYSIVP NLKVDISKCG SQVFTVGDQK
     FEVEVIDSVE HYVSYMKEIF DFNALKALIK GDITGKPFSI LINCLHGVTG PYAKQIFVKE
     LGAPSDSVVN AVPLEDFGGH HPDPNLTYAA DLVNAMKAGE YDFGAAFDGD GVRNMILGKK
     AFFVTPSDSL AVLAANLDCI PYSKQSGVKG FARSMPTGAA VDRVGKKLGK DVYEVPTGWK
     YFGNLMDAGK LSLCGEESFG TGSDHIREKD GVWAALAWLS VIASLKKSVE EILKDHWATY
     GRNYFTRYDY ENCESDPCNK MMAELETLVT SEAFKGKELS SNGRKYVVKL CDNFQFTDLI
     DGSVATKQGI RVLFEDGSRI VYRLSGTGSS GATVRVYIES YEPKEYTGEP QVVLKPLISL
     ALELARLQEF TGRDKPTVIT
//
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