ID A0A0M0K746_9EUKA Unreviewed; 677 AA.
AC A0A0M0K746;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=Ctob_012689 {ECO:0000313|EMBL:KOO34213.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO34213.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO34213.1}.
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DR EMBL; JWZX01001294; KOO34213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0K746; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
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 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:SF2; PHOSPHOGLUCOMUTASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..677
FT /note="phosphoglucomutase (alpha-D-glucose-1,6-
FT bisphosphate-dependent)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005602441"
FT DOMAIN 89..233
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 277..390
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 399..507
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 677 AA; 71522 MW; B251FA6B23A6A801 CRC64;
MMNLCLLRGV VLLSALLLSE SADASKAAVP VAAVPSMSHR REAVLQSSSL QSSPLLRLSG
GSVSGASALQ QRTAVLAPRV VPTEPHEGQK PGTSGLRKKT KVFQRPNYLE NFVQSIFDSL
PEGQLNGATL VVSGDGRYHN AAAIQTICQM AAANGVARVW VGVGGLLSTP AVSAVIRERE
GGVAVGGIVL TASHNPGGPD EDFGIKYNVQ NGGPALEAFT DAVHKRTNTL SEYRISDQLP
EVDLSIAARH VFTEVTGEGA AAAKRTFEVE VIEPTEDYVA LLRRCFDMDA IRTLLRREDM
SVVFDGMHGV AGPYAKAVLC GELGLPSSCL HHCEPSETFN GGHPDPNLVY AHELVATMGV
TAAGGAAPSA SSAPVFGAAA DGDADRNMIL GRGFFVTPSD SLALIAAHAH LIPWFANAGG
LKAVARSMPT SGAVDRVAAA QGLPFFETPT GWKFFGNLMD SRLLGGATLD PLLCGEESFG
TGSSHVREKD GLWAVLAWLT ILAEHNRQTP IGALVGVGDI VRQHWAHFGR NYYARYDYEG
VDANGAARVL ERLRGVSAMF TLAGHGPDRP QPLGTSGCAL ATADEFEYHD PVDKSVSKRQ
GVRLLFADGS RIIFRLSGTG SVGATIRIYL ERYMPATAPA EQLALETADA LAPLINLALE
LSQVHELTGR DAPTVIT
//
