ID D2V2S1_NAEGR Unreviewed; 568 AA.
AC D2V2S1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=NAEGRDRAFT_82954 {ECO:0000313|EMBL:EFC48945.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC48945.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48945.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; GG738849; EFC48945.1; -; Genomic_DNA.
DR RefSeq; XP_002681689.1; XM_002681643.1.
DR AlphaFoldDB; D2V2S1; -.
DR STRING; 5762.D2V2S1; -.
DR EnsemblProtists; EFC48945; EFC48945; NAEGRDRAFT_82954.
DR GeneID; 8855136; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_82954; -.
DR eggNOG; KOG0625; Eukaryota.
DR InParanoid; D2V2S1; -.
DR OMA; WIQDRAN; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000006671; 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; 2.
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:UP000006671}.
FT DOMAIN 17..174
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 568 AA; 63083 MW; EA259BC37C8675D0 CRC64;
MAPLTIRKQA TQPIPGQKMG TSGLRVKVKL VENTPSFLEN FSQSVFNIIL SSEQGLIGKV
NDQGCLQMVI GGDGRYYNKK AIQTILKILY ANAVARNLKI HVRVGQDGVV STPAVSCMIR
KYKAELGGLI LTASHNPGGP NNDWGIKYNA PNGGPAPEKI TDIIYQQSTQ ITEYHTCDEF
PEIDFSHISD VFSDEHLKVS VIDPVDDYYE LLSTIFDMEK IKKLIQRDDF NLLFDAMHGV
TGPYAKRILH EKLGADPQKN LINYVPSEDF GKGHPDPNLT YAEELVKKVL NDENSIIDLG
AASDGDGDRN MILGKHFFVT PSDSVAIIAD YAQRCIPYFQ KSGISGLARS MPTSTALDRV
AKALGVNIYE VPTGWKYFGN LFDAGKLSIC GEESFGTGSD HIREKDGMWA VLSWLSIMAF
ENENTKTSVA DIVKNHWKKY GRSYYTRYDY EEVSSEGANN MMSHIRDTYL FESLSVASCE
EFSYTDPIDN SFTGKQGMIF KLVDQSRIVF RLSGTGSSGA TVRVYMEKYN PDRLDGNPLE
EVKPLAHVAL TVSKLAEFTG RNEPTVIT
//
