ID   A0A074VFU9_9PEZI        Unreviewed;       577 AA.
AC   A0A074VFU9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Phosphoglucomutase-2 {ECO:0000313|EMBL:KEQ59353.1};
GN   ORFNames=M437DRAFT_56839 {ECO:0000313|EMBL:KEQ59353.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ59353.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ59353.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ59353.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; KL584848; KEQ59353.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074VFU9; -.
DR   STRING; 1043003.A0A074VFU9; -.
DR   HOGENOM; CLU_016950_0_1_1; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000030672; 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:InterPro.
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   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030672}.
FT   DOMAIN          45..182
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..313
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          322..431
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   577 AA;  63521 MW;  7CDBEA2C4CB1A661 CRC64;
     MDSSLQTYVD EWLRLDQDVS TRSEIERLVA ENNTTELTLR LQKRIAFGTA GLRGRMEAGF
     SRMNSLTVIQ ASQGLAEYLL KTNHDTRTQG VVIGRDARHN SDKFAKLVAA VFVAKAIPVK
     WLGQVHTPLV PYTVGHLNSA AGVMITASHN PAADNGYKVY WGNGCQIVPP HDAGIAASID
     ANLEPITWDV DILEQGSPLV TNALHQVQQG YMATVANLSA VSNPDASVPF VYTPMHGVGL
     PFFTSVMELL GLESKMHVVQ EQAHPNPDFP TVRFPNPEEK GALDLAKQVA DHNGIKLILA
     NDPDADRFAA AENVDGEWRQ LTGNQMGVLL ASHILDTYQP TQSSKGLAML SSTVSSKMLA
     GMATASGKFH WEETLTGFKW LGNRSRELQQ QDYDALFAYE EAIGYMFSEV VFDKDGVAAA
     AVFLAACDRW NKQGLSPWAK YNELCKQYGY FEDANTYVIS PSSDVTNVVF EQIRQAKPTT
     VGSRKILRWR DLTIGFDSAT PDNKPTLPVD KSSQMISCEL AGNVHFTVRG SGTEPKIKFY
     IEGSASSSQE ARTSAQEVLE DLMKEWFKPE VHGLKRE
//