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Database: UniProt
Entry: A0A1X2HQP2_SYNRA
LinkDB: A0A1X2HQP2_SYNRA
Original site: A0A1X2HQP2_SYNRA 
ID   A0A1X2HQP2_SYNRA        Unreviewed;       550 AA.
AC   A0A1X2HQP2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=BCR43DRAFT_530033 {ECO:0000313|EMBL:ORZ01698.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ORZ01698.1, ECO:0000313|Proteomes:UP000242180};
RN   [1] {ECO:0000313|EMBL:ORZ01698.1, ECO:0000313|Proteomes:UP000242180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORZ01698.1,
RC   ECO:0000313|Proteomes:UP000242180};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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 phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORZ01698.1}.
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DR   EMBL; MCGN01000002; ORZ01698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2HQP2; -.
DR   STRING; 13706.A0A1X2HQP2; -.
DR   InParanoid; A0A1X2HQP2; -.
DR   OMA; IWVGQNG; -.
DR   OrthoDB; 5476118at2759; -.
DR   Proteomes; UP000242180; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03085; PGM1; 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   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; IPR045244; PGM.
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   PRINTS; PR00509; PGMPMM.
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:UP000242180}.
FT   DOMAIN          15..154
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          207..289
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          301..414
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   550 AA;  60593 MW;  0B079EE9905C70B8 CRC64;
     MVNTITVPTQ PYDGQKPGTS GLRKRVKVFM QKNYTENFIQ AVLQAVEGGA QGATLVVGGD
     GRYYLDEVMQ IIIKFSAAAG VQKLIIPRDG LVSTPAGSHL IRKYQATGGL LLTASHNPGG
     PDKDFGIKYN VRNGGPAPEN VTNHIYELSK KLTELTYADI PHVDYSKLGS QKVGDMTIDV
     IDGIEDYVIL MKEIFDFHAI KTFLDGHPEF KVLFDGMHGV TGIYGQRLFL QEFGLSKSSV
     MRATPLPDFG GDHPDPNLVY AHELVEQVNK NNIDFGAASD GDGDRNMIIG KDNAFVTPSD
     SVAVIAHYAR EAIPYFRKHG LAGLARSMPT SRALDRVAQA QGLDIYEVPT GWKFFGNLMD
     ANKCSLCGEE SFGTGSDHVR EKDGVWAILA WLSIVVHVKN PSIEAILQDH YRRYGRNFFS
     RYDYEEVESD AANAMIDALR GQLGSLKGQT INRYTIDYAD DFSYTDPIDG STSSHQGLRV
     LFTDGSRFVV RLSGTGSQGA TIRLYVEKYS DDPSEYATDT QTALKPLIDV ALELTRLQHF
     TGRYTPTVIT
//
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