ID W5M2Y0_LEPOC Unreviewed; 626 AA.
AC W5M2Y0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Phosphoglucomutase 2 like 1 {ECO:0000313|Ensembl:ENSLOCP00000002738.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002738.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002738.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AHAT01003315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015197172.1; XM_015341686.1.
DR RefSeq; XP_015197173.1; XM_015341687.1.
DR RefSeq; XP_015197174.1; XM_015341688.1.
DR RefSeq; XP_015197175.1; XM_015341689.1.
DR RefSeq; XP_015197176.1; XM_015341690.1.
DR AlphaFoldDB; W5M2Y0; -.
DR STRING; 7918.ENSLOCP00000002738; -.
DR Ensembl; ENSLOCT00000002744.1; ENSLOCP00000002738.1; ENSLOCG00000002326.1.
DR GeneID; 102693679; -.
DR CTD; 283209; -.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000158353; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; W5M2Y0; -.
DR OMA; GYCVDPE; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000002326; Expressed in brain and 13 other cell types or tissues.
DR GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IBA:GO_Central.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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 PANTHER; PTHR45745:SF2; GLUCOSE 1,6-BISPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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 Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 62..206
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 235..339
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 351..472
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 626 AA; 70591 MW; 802B040A22617010 CRC64;
MGEYGGDLNA NLLCPDTGDP QLDKAVVQWM TWDQNPQTRA QIESLAREGK RQELRERLCS
RMTFGTAGLR APMGAGFALI NDLTVIQSTQ GMHRYLEKSF PDLRRRGVVI GYDTRGQEAS
NCRSERLARL AAAVLLSRNV PVFLFSTYVP TPFVPYAVRK LGTAAGVMVT ASHNPKEDNG
YKVYWKNGAQ IASPHDKEIL KCIEESLEPW SDSWKENLAD SSDLRSDPLE KICRSYMEDL
KLVCFHRELN TKTPLKFVHT AFHGVGHEYV QQAFRVFGFL PPLPVPEQKD PDPEFSTVRS
PNPEEGESVL ELSLRLAEKE GARVVVATDP DADRLAVAEQ YEPGRWKVFT GNEMAALLGW
WLFWNWREKH ADMADLDRVY MLATTVSSKI LRTIARREGF HFEETLPGFK WIGNRVKELM
DKGNEVLFAF EESIGFMCGT SVLDKDGVSA AVVVAEMAAY LETRNFTMTQ QLAHIYEVYG
LHISETSYLI CHDPPTVNRI FARLRNFGGE VRYPLSCGEH SITHIRDVTT GYDSSQRSGK
SVLPIAKNSQ MVTFTFQNGS VATLRTSGTE PKIKYYAELC AAPGKSDLSS MREELRKLTA
ALVEDFLEPD RNNLTRRSSR ESEKLL
//
