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
//