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Database: UniProt
Entry: A0A0A2WDQ7_BEABA
LinkDB: A0A0A2WDQ7_BEABA
Original site: A0A0A2WDQ7_BEABA 
ID   A0A0A2WDQ7_BEABA        Unreviewed;       796 AA.
AC   A0A0A2WDQ7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KGQ11279.1};
GN   ORFNames=BBAD15_g2980 {ECO:0000313|EMBL:KGQ11279.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11279.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ11279.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11279.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) 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:KGQ11279.1}.
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DR   EMBL; ANFO01000228; KGQ11279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2WDQ7; -.
DR   STRING; 1245745.A0A0A2WDQ7; -.
DR   HOGENOM; CLU_353007_0_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 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; 1.10.1220.10; Met repressor-like; 1.
DR   Gene3D; 1.20.1380.10; Replication modulator SeqA, C-terminal DNA-binding domain; 1.
DR   HAMAP; MF_00908; SeqA; 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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR   InterPro; IPR045244; PGM.
DR   InterPro; IPR005852; PGM_a-D-Glc-sp.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   InterPro; IPR005621; SeqA.
DR   InterPro; IPR026577; SeqA_DNA-bd_C.
DR   InterPro; IPR036835; SeqA_DNA-bd_C_sf.
DR   InterPro; IPR033761; SeqA_N.
DR   NCBIfam; TIGR01132; pgm; 1.
DR   PANTHER; PTHR22573:SF57; 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; PF00408; PGM_PMM_IV; 1.
DR   Pfam; PF03925; SeqA; 1.
DR   Pfam; PF17206; SeqA_N; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   SUPFAM; SSF82808; Replication modulator SeqA, C-terminal DNA-binding domain; 1.
DR   SUPFAM; SSF47598; Ribbon-helix-helix; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA replication inhibitor {ECO:0000256|ARBA:ARBA00022880};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   DOMAIN          1..36
FT                   /note="Negative modulator of initiation of replication SeqA
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17206"
FT   DOMAIN          72..180
FT                   /note="Replication modulator SeqA C-terminal DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03925"
FT   DOMAIN          196..335
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          366..473
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          476..595
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          645..695
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   796 AA;  87195 MW;  8D07FE4B6A11E470 CRC64;
     MKTIEVDDEL YRYIASQTKH IGESASDILR RMLKFTAGQT PAATPTPAAP ERAAAPVVEE
     KPANTARNRV RAVRELLLSD EYAAQNKAVN RFMMVLSTLY QLDAKTFGEA TESLHGRTRV
     YFAGDEQTLL ANGNQTKPKH VPGTPYWVIT NTNTGRKCSM IEHIMQSMQF PAELIEKLTA
     QYYVLKPVVG NSEHAVKFGT SGHRGSAARH SFNEPHILAI AQAIAEERAK NGITGPCYVG
     KDTHALSEPA FISVLEVLAA NGVDVIVQQD NGYTPTPAVS NAILVHNQKG GAQADGIVIT
     PSHNPPDDGG IKYNPPNGGP ADTNVTKVVE DRANALLADG LKGVKRISLD KAWESGHVQE
     QDLVQPFIEG LVDIVDMAAI QKAGLKLGVD PLGGSGIEYW HRIAKHYNLD LTIVNDQVDQ
     TFRFMHLDKD GAIRMDCSSE CAMAGLLALR DKFDLAFAND PDYDRHGIVT PAGLMNPNHY
     LAVAINYLFQ HRPQWGKDVA VGKTLVSSAM IDRVVEDLGR KLVEVPVGFK WFVDGLFDGS
     FGFGGEESAG ASFLRFNGTP WSTDKDGIIM CLLAAEITAV TGKNPQQHYD ELAARFGAPS
     YNRIQAPATS AQKAALSKLS PEMVSADTLA GDPITARLTA APGNGASIGG LKVMTENGWF
     AARPSGTEDA YKIYCESFLG AEHREQIEKE AVEIVSEVLK NANHHQRAAG DKRHAYPGNQ
     RHFLTKQNHR QNHRKDYAQL IDRGDLRHFP VFDCHKIEQP GQRPGHAAQQ NKQQRFFIGK
     DRADEVQFSL NDNHSH
//
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