ID A0A3Q1H1F8_9TELE Unreviewed; 564 AA.
AC A0A3Q1H1F8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphoglucomutase-1-like {ECO:0000313|Ensembl:ENSAPOP00000033552.1};
GN Name=PGM1 {ECO:0000313|Ensembl:ENSAPOP00000033552.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000033552.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000033552.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR AlphaFoldDB; A0A3Q1H1F8; -.
DR STRING; 80966.ENSAPOP00000033552; -.
DR Ensembl; ENSAPOT00000028577.1; ENSAPOP00000033552.1; ENSAPOG00000000630.1.
DR GeneTree; ENSGT00940000155542; -.
DR InParanoid; A0A3Q1H1F8; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000257200; Unplaced.
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:SF60; 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 19..160
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 198..305
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 323..424
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 564 AA; 62635 MW; 403CE3B143195947 CRC64;
MENSPLQLLT VPTAPYPDQR PGTSGLRKKV YVFQSRRNYL HNFIQSIFSS IDLRDRQGST
MVVGGDGRFF NRTAIEVIVQ MAAANGVGRM IIGHHGILST PAISCLIRKY KAIGGIVLTA
SHNPGGPDGD FGIKFNTANG GPAKEAVTSK IFQISRTIEE FAICPGLRVD LTTLGKQMFD
LENKFKPFTV EIVDSVESYA NLLRNIFDFA ALKELLSGEN HIKIRIDAMH GVAGPYVRKI
MCEELGCPVN SAINCVPLED FGGQHPDPNL MYATDLVDSM RDGQYDFGAA FDGDGDRNMI
LGKRGFFVTP SDSVAVIADN IFCIPYFQHT GVRGFARSMP TSAALDRVAK ATKIELYETP
TGWKFFGNLM DAGMLSLCGE ESFGTGGDHI REKDGLWAVL AWLSILATRK QSVEDIVKDH
WLKYGRNYFT RYDYENVDID AACEMMEDLE IMIADKSFVK QRFAVEDKIY QVEKADNFEY
TDPVDSTISR NQGLRIIFSD GSRIIYRLSG TGSDGATVRI YIDSYEKEQI FEDTQVMLAP
LATIALKISQ LHHRMGRSGP SVIT
//
