ID G4YID5_PHYSP Unreviewed; 1058 AA.
AC G4YID5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGZ27518.1};
GN ORFNames=PHYSODRAFT_554034 {ECO:0000313|EMBL:EGZ27518.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ27518.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ27518.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ27518.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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 UDPGP type 1 family.
CC {ECO:0000256|ARBA:ARBA00010401}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; JH159151; EGZ27518.1; -; Genomic_DNA.
DR RefSeq; XP_009514793.1; XM_009516498.1.
DR AlphaFoldDB; G4YID5; -.
DR STRING; 1094619.G4YID5; -.
DR EnsemblProtists; EGZ27518; EGZ27518; PHYSODRAFT_554034.
DR GeneID; 20662963; -.
DR KEGG; psoj:PHYSODRAFT_554034; -.
DR InParanoid; G4YID5; -.
DR OMA; DSAEHHV; -.
DR Proteomes; UP000002640; 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:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR CDD; cd00897; UGPase_euk; 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 InterPro; IPR016267; UDPGP_trans.
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:UP000002640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 491..635
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 675..788
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 797..923
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 1058 AA; 115432 MW; 1F41AF0850EFB069 CRC64;
MAPFDAYRAK MQAAGLSTEA IKAFEYSYDA LVSGETGMIA EDSIKPADNL PYLENKEGSI
RESVKADPEL LKETVVLKLN GGLGTSMGLD KAKSLLTVKG DDTFLDIMAK QVTELRATHK
SNVRFVLMNS FSTSADTLEY LQKYPELVED EALELLQNKV PKVNAATMEP ATYAANPAKE
WCPPGHGDLY ASLAGSGKLD KLVAEGVKYM FVSNSDNLGA TLDLDLLTYF AQSGKPFLME
CCERTENDKK GGHLAERTAD GRLILRESAQ CADEDEKEFQ NITKHRYFNT NNLWIRLDKL
QEELKKQGGV IRLPMIKNSK TVDPKDSSST PVFQLETAMG AAIECFDGAG AVCVPRTRFA
PVKKCDDLIL LRSDAYVITE DYRPVIAPER EGVAPIVSLD SKNFKLVQQL EAAVRGNVPS
LIKCDRLKIV GNVGFAPGVV FDGSVEVVNK SSEQKTVLAG TYKDTTVDLT EQKGLGKLKV
TTVKTSPFQD QKPGTSGLRK KTKTFMSDNY LQNFVASVFE ALPAKDLNGG TLVVSGDGRY
FNKEAIQIII KMAVAYGVDR LWIGKDGLLS TPCVSAVVRE REGGSVAFGA FILSASHNPG
GPNEDFGIKY NCENGGPAPE KVTNEIFALS KVITSYKIAA DFPTVDVTKI GTTSVASDDG
SRTITVEVFD SAEHHVDLLK QIFDFHAIKK LVSREDFTFV VDAMSGVNGP YARRVFVEEL
GCNESCLQNA SPLEDFGGGH ADPNLTYAKA LIKVMGVDAK GLPVTGQEQE PPSFGAAWDG
DADRNMILGS RFFVTPSDSL AIIAANCTVI PFFKNGLRGV ARSMPTSGAV DLVAKKLNVP
FFEVPTGWKF FGNLMDSHVV FGKEDYTPFI CGEESFGTGS NHIREKDGMW AVLAWLSILA
SKQVDGAPLV TVEDIVRDHW KKYGRNYYCR YDYENVDKAA AEGMFAEMTK FDVVVGKEIN
GFKVEKADEF EYVDPVDGSV SSHQGIRFLF EGGSRVVFRL SGTGVAGATI RMYVEKYEEP
TGNLDQNAAA ALEKLIEVGL KLSDLEKKTG RKAPTVIT
//
