ID U3JQ86_FICAL Unreviewed; 782 AA.
AC U3JQ86;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Phosphoglucomutase 2 like 1 {ECO:0000313|Ensembl:ENSFALP00000004940.2};
GN Name=PGM2L1 {ECO:0000313|Ensembl:ENSFALP00000004940.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000004940.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000004940.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR AlphaFoldDB; U3JQ86; -.
DR STRING; 59894.ENSFALP00000004940; -.
DR Ensembl; ENSFALT00000004964.2; ENSFALP00000004940.2; ENSFALG00000004747.2.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000158353; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000016665; Unplaced.
DR GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IEA:Ensembl.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 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 SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 225..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 398..504
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 514..629
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..123
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 86610 MW; FC6DB1DC3883C127 CRC64;
MLSPGSAWQQ GGHTRRTARS DPIPVGSCRS APSCSCSCSC SCSSQLGLIL GACGGHGRQQ
PDGGLAAKPA GSADRPEPEP AGGRALPRPA PARRPRRPRP QRQRLHVHPV RHDALRRHRG
QPHPGLHPLP QGGQAQRPLP RLHQEQGLHD PALPRSLPAA MGDCGAPGDV NSNVLVARST
GDAQLDKAVW QWLSWDKNQK TKAQIERLLQ DGKHRELRER LCCRLSFGTA GLRSAMGAGF
CYINDLTVIQ STQGIYKYLE RNFSDFKQRG FVVGYDTRGQ VTSNCSSKKL AKLTAAVLLA
KDVPVYFFST YVPTPFVPYA VQQLGAVAGV MITASHNRKE DNGYKVYWEN GAQITSPHDK
EIIKCIEECV EPWSGSWNEN LVDTSPLRQD PLKKICDSYM EDLTKICYHR ELNVQSSLKF
VHTSFHGVGH DYVQLAFQAF GFQPPIPVPE QKDPDPDFST VKCPNPEEGE SVLELSLRLA
EKEGAKVVVA TDPDADRLAV AEQQENGSWK VFTGNELAAL FGWWMFSCWK ENCSPDADVR
NVYMLATTVS SKILRAIALK EGFHFEETLP GFKWIGSRVK NLLDNGKEVL FAFEESIGFM
CGTSVLDKDG VSAAVVIAEM ATYLQGQSLT LAQKLLGIYE TYGYHISKTS YFLCYDPATI
KRIFERLRNW DGPQCYPQCC GVYSILHVRD VTTGYDSSQP DQQSVLPVSR SSQMITFTFQ
NGCVATLRTS GTEPKIKYYA EMCALPGHSD RAVLEEELQR LVEALVENFL EPAKNGLTWR
SA
//