ID W5PJB6_SHEEP Unreviewed; 595 AA.
AC W5PJB6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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|Ensembl:ENSOARP00000010537.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000010537.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000010537.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000010537.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000010537.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMGL01002006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01002007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01002008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PJB6; -.
DR SMR; W5PJB6; -.
DR STRING; 9940.ENSOARP00000010537; -.
DR PaxDb; 9940-ENSOARP00000010537; -.
DR Ensembl; ENSOART00000010693.1; ENSOARP00000010537.1; ENSOARG00000009826.1.
DR eggNOG; KOG0625; Eukaryota.
DR HOGENOM; CLU_009330_0_1_1; -.
DR OMA; WIQDRAN; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000009826; Expressed in longissimus thoracis muscle and 54 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356}.
FT DOMAIN 48..190
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 227..332
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 340..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65243 MW; 2848685A9746A9AC CRC64;
FKEEGRAQPV WPRPRPCSHP RAAAATARKQ VATMVKIVTV KTKAYQDQKP GTSGLRKRVK
VFQSSSNYAE NFIQSIISTV EPAQRQEATL VVGGDGRFYM KEAIQLIVRI AAANGIGRLV
IGQNGILSTP AVSCIIRKIK AIGGIILTAS HNPGGPNGDF GIKFNISNGG PAPEAITDKI
FQISKTIEEY AICPDLHVDL GVLGKQQFDL ENKFKPFTVE IVDSVEAYAT MLRNIFDFNA
LKELLSGPNR LKIRIDAMHG VVGPYVKKIL CEELGAPANS AVNCVPLEDF GGHHPDPNLT
YAADLVETMK TGEHDFGAAF DGDGDRNMIL GKHGFFVNPS DSVAVIAANI FSIPYFQQTG
VRGFARSMPT SGALDRVANA TKIALYETPT GWKFFGNLMD ASKLSLCGEE SFGTGSDHIR
EKDGLWAVLA WLSILATRKQ SVEDILKDHW QKYGRNFFTR YDYEEVEAEG ANKMMKELEA
LISDRSFVGK QFPVGDKVYT VEKIDNFEYS DPVDGSISRN QGLRLLFADG SRIIFRLSGT
GSAGATIRLY IDSYEKDLAK IYQDPQVMLA PLISIALKVS QLQEKTGRTA PTVIT
//
