ID   U1Q515_9ACTO            Unreviewed;       485 AA.
AC   U1Q515;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Putative phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:ERH17611.1};
GN   ORFNames=HMPREF1978_00451 {ECO:0000313|EMBL:ERH17611.1};
OS   Actinomyces graevenitzii F0530.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1321817 {ECO:0000313|EMBL:ERH17611.1, ECO:0000313|Proteomes:UP000016481};
RN   [1] {ECO:0000313|EMBL:ERH17611.1, ECO:0000313|Proteomes:UP000016481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0530 {ECO:0000313|EMBL:ERH17611.1,
RC   ECO:0000313|Proteomes:UP000016481};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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, 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:ERH17611.1}.
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DR   EMBL; AWSC01000014; ERH17611.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1Q515; -.
DR   PATRIC; fig|1321817.3.peg.391; -.
DR   HOGENOM; CLU_016950_7_1_11; -.
DR   Proteomes; UP000016481; 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; cd05800; PGM_like2; 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; IPR005843; A-D-PHexomutase_C.
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   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          17..147
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          177..276
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          281..392
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          439..479
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   485 AA;  53360 MW;  E13ED6C1528DEE22 CRC64;
     MMTEELKTYT AQEPQIHFGT GGWRAIISEG FTQLNVQRVA QALAARIISQ GVVDKPVVIG
     YDQRFLSPEF AWWSAQVLAA NGIHVHLIDR PAPTPMIMWT VKDLGCAYGM AITASHNPAI
     YNGIKVFTAG GRDAEVEITT PLQDAANALG ADDIKLIELS EAQAAGLIST QTSMNWYIDS
     ILDSVDVKAI RHAHLKIVLD PMFGVSRTCL QTILMTARCD VETIHERRDT LFGGRLPSPS
     SKTLHALANE VLERGAAMGI ATDGDADRLG VIDNTGKFLH PNEILVLLYE YLLEEKGWHG
     PVVRNLATTH LLDRVARAHG EQCYEVPVGF KWVSSKMAEH DAIIGGESSG GLTVKGHIAG
     KDGVYAGTLL VEMVAKKGKH LSEIYADIVA KYGQLEMIET DYGFTMERKA QLLEQIYERH
     DLPEFAQAVD HVSYLDGCKV YFADDSWVVI RFSGTEPLLR VFAEAATYEQ AQGIIDQVVA
     YYQLA
//