ID F9PLX3_9ACTO Unreviewed; 472 AA.
AC F9PLX3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I {ECO:0000313|EMBL:EGV12539.1};
GN ORFNames=HMPREF9058_1107 {ECO:0000313|EMBL:EGV12539.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV12539.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV12539.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV12539.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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:EGV12539.1}.
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DR EMBL; AFUR01000006; EGV12539.1; -; Genomic_DNA.
DR RefSeq; WP_009747812.1; NZ_AFUR01000006.1.
DR AlphaFoldDB; F9PLX3; -.
DR eggNOG; COG1109; Bacteria.
DR Proteomes; UP000004281; 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 3..133
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 163..262
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 267..378
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 421..465
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 472 AA; 51195 MW; 0B7E3F1E60D4D3A8 CRC64;
MIHFGTGGWR AVIGDEFTRA NVRLLTQGLA NRILEEGTSE QGVVIGYDRR FLSDTAAWWA
IEVLVGNGIR VTLIDRPSPT PTTMWTVRRL GAAYGMAVTA SHNPALYNGI KIFLPGGRDA
DQAVTDELTA SLHGLTDADV RSVEPHEARS SELVTIQRSI NWYLDAIIDK LDTETIRHAH
MHIVLDPMFG VSETSLQTIL LTARCQVDVI HDRHDPLFGG RMPSPTEGTV TTLRNAVVES
GADLGIATDG DADRLGIIDD TGAYLTPNQV LVLLYDYLLT RKGWSGPAVR NMSTTHLLDR
VAAAHGQVCY EVPVGFKWIS AKMAETGAVI GGESSGGLTV RGHIPGKDGV YAGSLLVEAV
AASGKRLSEL YADIVARYGE LVMVENAYGF TSERRAELEE RIFGAHDLPA FTHDVERVSW
QDGCKVYFAC GGWVTIRFSG TEPLLRVFTE MPTGDEARAT AAAVASHYGL DA
//
