ID M4BKZ0_HYAAE Unreviewed; 1058 AA.
AC M4BKZ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:HpaP807074};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP807074, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP807074}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP807074};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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; JH598368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BKZ0; -.
DR STRING; 559515.M4BKZ0; -.
DR EnsemblProtists; HpaT807074; HpaP807074; HpaG807074.
DR VEuPathDB; FungiDB:HpaG807074; -.
DR eggNOG; KOG0625; Eukaryota.
DR eggNOG; KOG2638; Eukaryota.
DR HOGENOM; CLU_008043_0_0_1; -.
DR InParanoid; M4BKZ0; -.
DR OMA; DSAEHHV; -.
DR Proteomes; UP000011713; 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:UP000011713};
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..922
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 1058 AA; 115600 MW; ABA50B89D3A0FD08 CRC64;
MAQFDVFRAK MQAAGLSTEA IKAFEYSYEA LVSGETGMIT EASIKSVDDL PYLENKAGSI
RESIKADPAL LKETVVLKLN GGLGTSMGLD KAKSLLTVKG DDTFLDIMAK QVTELRSAHK
SHVRFVLMNS FSTSADTLEY LQKYPELVED ETLELLQNKV PKVDVSNMEP ALYSSNPSKE
WCPPGHGDLY ASLAGSGKLD KLVADGVKYM FVSNSDNLGA TLDLDLLTYF AQSGKPFLME
CCERTENDKK GGHLAERTAD GRLVLRESAQ CADEDEKEFQ DIAKHRYFNT NNLWIRLDKL
QEELKQQGGV IRLPMIKNSK TVDPKDSSST PVFQLETAMG AAIECFDGAG AVCVPRTRFA
PVKKCDDLIL LRSDAYVITE DYRPIIAPER EGVAPIVSLD SKHFKLVQQL EAAVRGNVPS
LIKCDRLKIT GNVGFAAGVV FEGSVEVVNK SSEQKTVLAG TYKDTVVDLS KQKGLGKLKV
TTVKTTPFQD QKPGTSGLRK KTKTFMSDNY LQNFVASVFD ALPAKDLNGG TLVVSGDGRY
FNKDAIQIVI KMAVAYGVDR LWIGKDGLLS TPCVSAVVRE REGGSVAFGA FILSASHNPG
GPDEDFGIKY NCENGGPASE KVTEEVYALS KVITSYKIAS EFPTIDIAKI GTTSVVADDE
SRTITVEVFD SAEHHVDLLK QIFDFHAIKK LVSRSDFSFV VDSMSGVNGP YARRVFVEEL
GCDESCLLNA TPMEDFNGCH ADPNLTYAKT LIKAMGVDAK GLPVLGQEQD PPSFGAAWDG
DADRNMILGS RFFVTPSDSL AIIAANCTVI PFFKNGLRGV ARSMPTSGAV DLVAKKLNVP
FFEVPTGWKF FGNLMDSNVV FGKEDYTPFI CGEESFGTGS NHIREKDGMW AVLSWLSILA
SKQVDGAPLV TVEDVVRDHW KKFGRNYYCR YDYENVDKAA AEVMFADMTK FDGVAGKEID
GFKIDKADEF EYVDPVDGSV SSHQGIRYLF EGGSRVIFRL SGTGVAGATV RMYIEKYEEP
TGNLGQNAAE ALEKLINVGL KLSDLQKKTG RSTPTVIT
//
