ID E7N7B2_9ACTO Unreviewed; 560 AA.
AC E7N7B2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Alpha-D-glucose phosphate-specific phosphoglucomutase {ECO:0000313|EMBL:QCT32169.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:EFW27950.1, ECO:0000313|EMBL:QCT32169.1};
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:EFW27950.1};
GN Name=pgm {ECO:0000313|EMBL:EFW27950.1};
GN ORFNames=FBF36_00600 {ECO:0000313|EMBL:QCT32169.1}, HMPREF9057_00665
GN {ECO:0000313|EMBL:EFW27950.1};
OS Actinomyces sp. oral taxon 171 str. F0337.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW27950.1, ECO:0000313|Proteomes:UP000005722};
RN [1] {ECO:0000313|EMBL:EFW27950.1, ECO:0000313|Proteomes:UP000005722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:EFW27950.1,
RC ECO:0000313|Proteomes:UP000005722};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCT32169.1, ECO:0000313|Proteomes:UP000310751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:QCT32169.1,
RC ECO:0000313|Proteomes:UP000310751};
RA Collins A.J., Murugkar P., Chen T., Dewhirst F.E.;
RT "Saccharibacteria TM7 and host bacteria genomes.";
RL Submitted (APR-2019) 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}.
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DR EMBL; AECW01000079; EFW27950.1; -; Genomic_DNA.
DR EMBL; CP040005; QCT32169.1; -; Genomic_DNA.
DR RefSeq; WP_009394277.1; NZ_GL637741.1.
DR AlphaFoldDB; E7N7B2; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_11; -.
DR Proteomes; UP000005722; Unassembled WGS sequence.
DR Proteomes; UP000310751; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR045244; PGM.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
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 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EFW27950.1};
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 38..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 217..331
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 335..455
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 492..554
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 301..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 58650 MW; 560BF2D29B6578AA CRC64;
MHPRAGQPAQ PEDLIDVDEV VSAYYDLVPD PAVPAQKVVF GTSGHRGSSL DTAFNEAHIV
ATTAAIVEYR RSQGTDGPLY LGRDTHALSE PAWRTAVEVL AGAGVTTAVD ARGAYTPTPA
VSHSILLANG AGTEAGVRTS GPGLADGIVV TPSHNPPRDG GFKYNPPTGG PAGSESTTWI
ANRANELLAS GWQDVPRVPV PEALDGPHVV KHDYLETYVA DLESVIDLEA IRKAGVRIGA
DPLGGASVDY WGAIGERYGL ELTVVNPEVD PAWHFMTLDW DGKIRMDCSS PNAMASLRST
MTPDAEGRTP YDVATGNDAD SDRHGIVTPD GGLMNPNHFL AVAIEYLFTH RPGWPADAAV
GKTLVSSSLI DRVAAAIGRT LIEVPVGFKH FVPGLLDGSI GFGGEESAGA SFLRKDGTVW
TTDKDGIILA LLASEIIAVT GKSPSQLHEE QVERFGASAY ARIDAAASKE EKAKLAALAA
EDVTATELAG QEITARLVDA PGNGAAIGGL KVTTEDAWFA ARPSGTEDVY KIYAESFQGA
DHLAQVQEEA KKVVSAALGG
//
