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Database: UniProt
Entry: G0Z3A1_PIG
LinkDB: G0Z3A1_PIG
Original site: G0Z3A1_PIG 
ID   G0Z3A1_PIG              Unreviewed;       562 AA.
AC   G0Z3A1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Phosphoglucomutase-1 {ECO:0000256|ARBA:ARBA00040178};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE   AltName: Full=Glucose phosphomutase 1 {ECO:0000256|ARBA:ARBA00043051};
GN   Name=PGM1 {ECO:0000313|EMBL:ADW94631.1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:ADW94631.1};
RN   [1] {ECO:0000313|EMBL:ADW94631.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Chen C., Zhu C.Y., Xiong Z.Y.;
RT   "Analysis of Sequence, Expression Patterns, and Polymorphism of The
RT   Differentially Expressed PGM1 Gene between Porcine Longissimus Doris.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC       of glucose. {ECO:0000256|ARBA:ARBA00003488}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; HQ877617; ADW94631.1; -; mRNA.
DR   RefSeq; NP_001233247.1; NM_001246318.1.
DR   AlphaFoldDB; G0Z3A1; -.
DR   GeneID; 397566; -.
DR   KEGG; ssc:397566; -.
DR   CTD; 5236; -.
DR   OrthoDB; 5476118at2759; -.
DR   Genevisible; G0Z3A1; SS.
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: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:SF37; PHOSPHOGLUCOMUTASE-1; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT   DOMAIN          15..157
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          194..299
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          307..420
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   562 AA;  61725 MW;  663200209B6C8D62 CRC64;
     MVKIVTVKTK AYQDQKPGTS GLRKRVKVFQ SSANYAENFI QSIISTVEPA HRQEATLVVG
     GDGRFYMKEA IQLIVRIAAA NGIGRLVIGQ NGILTTPAVS CIIRKIKTIG GIILTASHNP
     GGPNGDFEIK FNISNGGPAP EAITDKIYQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK
     FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE
     LGAPANSAEN CVPLEDFGGH HPDPNLTYAA DLVGTMKTGE HDFGAAFDGD GDRNMILGKH
     GFLVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ALYETPTGWK
     FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAFLAWLS ILATRKQSVE DILKDHWQKY
     GRNFFTRYDY EEVEAEGANK MMKELEALIS DRSFVGKQFP VGDKVYTVEK IDNFEYSDPV
     DGSISRNQGL RVIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDLAKIYQ DPQVMLAPLI
     SIALEMSQLQ ERTGRTAPTV IT
//
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