ID F0WCJ8_9STRA Unreviewed; 1096 AA.
AC F0WCJ8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein ALNC14_050580 {ECO:0000313|EMBL:CCA18915.1};
GN ORFNames=ALNC14_050580 {ECO:0000313|EMBL:CCA18915.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA18915.1};
RN [1] {ECO:0000313|EMBL:CCA18915.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA18915.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) 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 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; FR824104; CCA18915.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WCJ8; -.
DR EnsemblProtists; CCA18915; CCA18915; ALNC14_050580.
DR HOGENOM; CLU_008043_0_0_1; -.
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; cd03085; PGM1; 1.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 530..673
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 713..826
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 835..961
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 1096 AA; 120504 MW; 3E4F150AD6F1F61F CRC64;
MLTHSLSNNT FINASNRSLS RNSSPCDYFR NLRLSTTIMS GNFSQYRAKM EQEGLSEAAI
KAFEHSYQAL VSGDSGMIAE NSISSVDTLD YLEGKPGCIR ESVVADSKLL KETVVLKLNG
GLGTSMGLDK AKSLLNVKGD DTFLDLIAKQ VMELRQEHKS NVRFVLMNSF STSADTLEYL
QKYPELFEDK ELELLQNKVP KVDASTLAPA TYSVNSSKEW CPPGHGDLYP SLAGSGKLEK
LLSQGYKYMF VSNSDNLGAC MDLDMLTYFA QSGKPFLMEC CERTENDKKG GHLAKRNSDG
RLILRESAQC DGQDEKHFQD IGKHRFFNTN NLWIRLDKLA EELEAQGGLI RLPMIKNAKT
VDPKDPSSTP VFQLETAMGA AIESFAGAGA VCVPRSRFAP VKKCDDLLLL RSDAYVLTSD
SRPILAPERD GVAPIVSLDS KTFKLVQQLE ASLRGNTPSL IKCSRLKVTG DVCFAPDVVF
EGEVTVVNKS SEPKAVLSGT YKDMTVDLTE QKGLGKLKSK TVKTSPILEQ KPGTSGLRKK
TKTFMEGHYL HNFVQSVFDA LPSRDLYGGT LVVSGDGRYF NREAIQIIIK MAVASGVDRV
WLGQNGLLST PAVSAVIRER EGGSVAFGAF ILTASHNPGG PNEDFGIKYN CENGGPAPEK
LTNEIYNNTK TIQSFKIAHD FPDVDISKIG KTCYASEDKS RTITIEVFDV TEDHVNLLKK
IFDFEAIKKL FARKDFSFVY DSMWGVQGPY AHRVFVNELG ASASCLLNDT PKENFNGGHA
DPNLTYAKEL VKIMGLDCHG KPVPTEKNPP AFGAACDGDA DRNMILGSKF FVTPSDSLAI
IAANAHLIPF FNKRGLRGVA RSMPTSGAVD LVAKKLGIAL FEVPTGWKFF GNLMDSNEIY
GKEDYTPFIC GEESFGTGSN HIREKDGMWA VLAWLSILAS KQGDGPFVSV EAIVREHWKM
YGRNYYCRYD YESVDKNAAE SMFARMVKFK NIVGQKMNGF QVKVADEFTY SDPVDGSLSR
HQGIRYIFED GSRVVFRLSG TGVAGATIRM YIEKYESPNG NLDQDTATAL APLIDVGLTL
SKLVEATGRT TPTVIT
//
