ID   A0A1D2VQ13_9ASCO        Unreviewed;       622 AA.
AC   A0A1D2VQ13;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phosphoglucomutase, first 3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASCRUDRAFT_5625 {ECO:0000313|EMBL:ODV63674.1};
OS   Ascoidea rubescens DSM 1968.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Ascoideaceae; Ascoidea.
OX   NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV63674.1, ECO:0000313|Proteomes:UP000095038};
RN   [1] {ECO:0000313|Proteomes:UP000095038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KV454475; ODV63674.1; -; Genomic_DNA.
DR   RefSeq; XP_020049981.1; XM_020191179.1.
DR   AlphaFoldDB; A0A1D2VQ13; -.
DR   STRING; 1344418.A0A1D2VQ13; -.
DR   GeneID; 30964815; -.
DR   InParanoid; A0A1D2VQ13; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000095038; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05799; PGM2; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095038}.
FT   DOMAIN          46..193
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          227..332
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          346..463
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   622 AA;  70098 MW;  4C0E8DB553B416BC CRC64;
     MCEAEVSRLV ELWLEIDPNA ETRSEISNLY AAKEYNELRR RLAHRITFGT AGLRSSMEAG
     FNRMNDVTVL QASQGLAEYI KTSTLKLNAA ASSAKPTVVI GHDHRHHSKR FGDIAVSIFL
     LAGFKVYYLE DGAHDLVTTP MVPFAIDYLT ANGGIMITAS HNPAKDNGYK VYWSNACQII
     PPHDKNISLE ISQNLTPVKN AWKIAENISY HYKKGNLIYN KDLILEQYYK KLSGNLIFNK
     NINGLDNLPF IYTPMHGVGK EFALGVFNNV LNISSNVHFV DEQSLPDPSF PTVSFPNPEE
     KGALDLAIEI ANKKSIDIIV ANDPDADRFS AAVRIGDTHK FHQLTGNELG CLFANFIIEN
     LIEKSTNLKN VYLLNSTVSS EIIGSMSQKL GFNFTDTLTG FKWIGNKAIE LEEKGYLVPF
     GYEEAIGFMF NNVHDKDGIA ALTVFLQLIN SLVQKGTNVL DKLSEIYNNF GFFKEFNGYY
     KLKDISLIAE IFGNIRKFYN YENFNVGNEI IGNNKDFKIV YWRDLTIGFE TNARNNCPLL
     PVDPSSQMIT CILKPVNPQA EDEHIRLTCR GSGTEPKLKI YIEGKSDSEG RAKDLSITIW
     KLLKQEWFKP SFYNITEHCA DY
//