ID A0A0W8CPD2_PHYNI Unreviewed; 1035 AA.
AC A0A0W8CPD2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AM587_10001582 {ECO:0000313|EMBL:KUF85953.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF85953.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF85953.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF85953.1}.
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DR EMBL; LNFO01002381; KUF85953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8CPD2; -.
DR STRING; 4790.A0A0W8CPD2; -.
DR EnsemblProtists; KUF85953; KUF85953; AM587_10001582.
DR OMA; DSAEHHV; -.
DR Proteomes; UP000052943; 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:0070569; F:uridylyltransferase 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 Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR045244; PGM.
DR InterPro; IPR002618; UDPGP_fam.
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 Pfam; PF01704; UDPGP; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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:UP000052943};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 468..612
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 652..765
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 774..899
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 1035 AA; 113095 MW; 5E196D9EDFF0B8DA CRC64;
MAQFDAYRAK MQAAGLSTEA IKAFEYSYDA LVSGETGMIA ESSIKPADNL PYLENKADSI
RESVKADPSL LKETVVLKLN GGLGTSMGLD KAKSLLTVKG DDTFLDIMAK QVTELRATHK
SHVRFVLMNS FSTSADTLEY LQKYPEIVED ETLELLQNKV PKVNAATMEP ASYPANPAKE
WCPPGHGDLY ASLAGSGKLD KLVADGVKYM FVSNSDNLGA TLDLDLLTYF AQSGKPFLME
CCERTENDKK GGHLAERTAD GRLILRESAQ CADEDEKEFQ NIEKHRYFNT NNLWIRLDKL
QEELKKQGGV IRLPMIKNSK TCFDGAGAVC VPRTRFAPVK KCDDLILLRS DAYVITEDYR
PVIAPEREGV APIVSLDSKN FKLVQQLEAA VRGNVPSLIK CDRLKITGNV GFAPGVVFEG
SVEVVNKSSE QKTVLPGTYK DTTVDLTEQK GLGKLKVSTV KTSPFLDQKP GTSGLRKKTK
TFMSDNYLQN FVASVFEALP AKDLNGGTLV VSGDGRYFNK EAIQIIIKMA VAYGVDRLWI
GKDGLLSTPC VSAVVREREG GSVAFGAFIL SASHNPGGPN EDFGIKYNCE NGGPAPEKVT
NEVFALSKVI TSYKIAADFP TVDVTTIGTT TVDADDGSRT ITIEVFDSAE HHVDLLKQIF
DFHAIKKLVS RPDFTFVVDA MSGVNGPYAR RVFVEELGCD ESCLLNATPL EDFGGGHADP
NLTYAKTLIK AMGVDAKGLP VTGQEQEPPS FGAAWDGDAD RNMILGSRFF VTPSDSLAII
AANCTVIPFF KNGLRGVARS MPTSGAVDLV AKKLNVPFFE VPTGWKFFGN LMDSHVVFGK
EDYTPFICGE ESFGTGSNHI REKDGMWAVL AWLSILASKQ VEGAPLVTVE DVVRDHWKKF
GRNYYCRYDY ENVDKAAAEG MFADMTKFDG VVGKEINGFK VEKADEFEYV DPVDGSVSSH
QGIRFLFEGG SRVVFRLSGT GVAGATIRMY IEKYEEPTGN LDQNAAEALE KLIEVGLKLS
DLEKKTGRKA PTVIT
//
