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Database: UniProt
Entry: A0A1R0GNC9_9FUNG
LinkDB: A0A1R0GNC9_9FUNG
Original site: A0A1R0GNC9_9FUNG 
ID   A0A1R0GNC9_9FUNG        Unreviewed;       623 AA.
AC   A0A1R0GNC9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Putative phosphoribomutase {ECO:0000313|EMBL:OLY78369.1};
GN   ORFNames=AYI68_g7182 {ECO:0000313|EMBL:OLY78762.1}, AYI68_g7583
GN   {ECO:0000313|EMBL:OLY78369.1};
OS   Smittium mucronatum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY78369.1, ECO:0000313|Proteomes:UP000187455};
RN   [1] {ECO:0000313|EMBL:OLY78369.1, ECO:0000313|Proteomes:UP000187455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY78369.1,
RC   ECO:0000313|Proteomes:UP000187455};
RX   PubMed=27343289; DOI=10.1093/molbev/msw126;
RA   Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT   "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT   Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL   Mol. Biol. Evol. 33:2544-2554(2016).
RN   [2] {ECO:0000313|EMBL:OLY78369.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY78369.1};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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}.
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:OLY78369.1}.
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DR   EMBL; LSSL01006621; OLY78369.1; -; Genomic_DNA.
DR   EMBL; LSSL01005560; OLY78762.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R0GNC9; -.
DR   STRING; 133383.A0A1R0GNC9; -.
DR   Proteomes; UP000187455; 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   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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000187455}.
FT   DOMAIN          48..187
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          212..316
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          327..453
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   623 AA;  69569 MW;  D4ABBC530CE18847 CRC64;
     MTSSLSINDL VEKWLSYDKD PVTREQITKL NASGDVDSLE KLLRKPIEFG TAGLRSKMEA
     GFSRMNCVTV IQASQGLAVY VKKMVPDALK RGVVIGYDHR HNSQTFARLT AAVFLKHGFS
     VYFLDGLSPT PLVPFSVKKL LASCGVMITA SHNPKDDNGY KVYWENGAQI IPPVDGGIAE
     SIKQNQEITV WDLEAYKTDS KIISIRDKLI NEYLESAKYL ILDRDLNQKV NINYVYTAMH
     GVGAYFCERI LESLSLKPYI PVISQLQPDP DFPTVRFPNP EEKGALDLAK KAADENGSNI
     VLASDPDADR FAAAEKQEDG SWFVFSGDQL GILLAYYSLI LSKSKNLDVS KLAMVNSTVS
     SKMLRSMAKV EGFRFEDTLT GFKWMSNELI ALRDNEGLIP AFAYEEAIGF LLNPDILDKD
     GITALVSFVQ LANFLDHKGM KVKEFLDTLY TKYGYFASDN YYYICNDVPK INKIFDKIRY
     GDSTSDISDQ KRSNFLMESS GRRLKYPLNL GGSPITYIRD LTIGFEMSDF DKVSAASSNQ
     EFVIKSGQYY PKFMVSPSSQ MITFETANGG IITLRTSGTE PKIKYYCEIS GDNNDRESVA
     KELKQLVLSV GDDFLEAKAN GLV
//
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