ID A0A2Y9JKR7_ENHLU Unreviewed; 602 AA.
AC A0A2Y9JKR7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phosphoglucomutase-2 {ECO:0000313|RefSeq:XP_022361552.1};
GN Name=LOC111148982 {ECO:0000313|RefSeq:XP_022361552.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022361552.1};
RN [1] {ECO:0000313|RefSeq:XP_022361552.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022361552.1};
RG RefSeq;
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 RefSeq; XP_022361552.1; XM_022505844.1.
DR AlphaFoldDB; A0A2Y9JKR7; -.
DR STRING; 391180.A0A2Y9JKR7; -.
DR KEGG; elk:111148982; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000248482; Unplaced.
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 PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR PANTHER; PTHR45745:SF3; PHOSPHOPENTOMUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
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:UP000248482}.
FT DOMAIN 45..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 218..323
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 334..461
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 602 AA; 67470 MW; 678F50E4D51A240F CRC64;
MDTRLDQETA RWLRWDKNPL TLESAKQLIK DGNKEELQKC FGARMEFGTA GLRAAMGTGI
ARMNDLTIIQ TTQGFCRYLE KQFSDLKQRG VVISFDARAH PPSGSNSKRF ARLAATTFIT
QGIPVYLFSG ITPTPFVPYT VLHLKLCAGI MITASHNPKQ DNGYKVYWDN GAQITSPHDK
AISQAIEENL EPWPQAWDDS LINGSPLLRD PSASINESYF EDLKKYCFHR SVNRETKVQF
VHTSVHGVGH EFVQSAFKAF GFAPPEAVPE QKDPDPEFPT VKYPNPEEGK GVLTLSFALA
DKTKAKIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL LGWWLFTSWK EKNPDHSALK
DLYMLSSTVS SKILRAIALK EGFHFEETLT GFKWMGNRAK QLIDQGKNVL FAFEEAIGYM
CCPFVLDKDG VSAAVIIAEL ASFLATKNLS LSQQLKAIYV EYGYHITKAS YFICHDQGTI
KKLFENLRNY DGKNNYPKTC GRFEISGIRD LTTGYDDSQP DKKAVLPTSK SSQMITFTFA
NGGVATMRTS GTEPKIKYYS ELCAPPGNSD PEQLKKELNE LVSAIEEHFF QPQKYNLQPK
TE
//
