ID A0A1F1I8M5_9MICC Unreviewed; 574 AA.
AC A0A1F1I8M5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:OFR88014.1};
GN ORFNames=HMPREF2863_01125 {ECO:0000313|EMBL:OFR88014.1};
OS Micrococcus sp. HMSC067E09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=1739367 {ECO:0000313|EMBL:OFR88014.1, ECO:0000313|Proteomes:UP000177882};
RN [1] {ECO:0000313|EMBL:OFR88014.1, ECO:0000313|Proteomes:UP000177882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC067E09 {ECO:0000313|EMBL:OFR88014.1,
RC ECO:0000313|Proteomes:UP000177882};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OFR88014.1}.
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DR EMBL; LTYF01000047; OFR88014.1; -; Genomic_DNA.
DR RefSeq; WP_070637358.1; NZ_KV809409.1.
DR AlphaFoldDB; A0A1F1I8M5; -.
DR STRING; 1739367.HMPREF2863_01125; -.
DR Proteomes; UP000177882; Unassembled WGS sequence.
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 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 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};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000177882}.
FT DOMAIN 49..201
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 232..346
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 350..466
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 500..567
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 60663 MW; 64D96DDB7C396B5E CRC64;
MSETMHTPAV PAAQRPGTPA LPEDLIDVDA LLAAYTDRVP DPSDPAQKVV FGTSGHRGSS
LKTSFNDAHI AAITQAIVEY RATQGITGPV LVGKDTHALS APAQDTCVQV LLANDVPVMV
DSRGGYTPTP AVSHAILHLN AGRDLTPAGF SADGDNAGLA DGIVITPSHN PPSDGGLKYN
PPHGGPADTD ATGWIARRAN ELLTARLDGV RRLAPEEVEG HPRLDGFDFL DRYVSDLPKV
LDMDAIREAG VRIGADPMGG ASVDYWAEIG ARHGLELTVV NPEVDPRFGF MTLDWDGKIR
MDCSSPNAMA SLIERMTPDA EGNAPFDVAT GNDADADRHG IVTPDGGLMN PNHFLAVAID
YLYRKRSHWP QAAGVGKTLV SSSMIDRVAE SLDRELVEVP VGFKWFVPGL LTGSGVFGGE
ESAGASFVTL DGEPWTTDKD GMLLCLLAAE IIAVTGRSPS ELYRDLEALH GSPVYARIDA
PATAEQKARL KELSPEDVTV TELAGETILA ALTNAPGNSA PIGGLKVVTQ NAWFAARPSG
TEDVYKIYAE SFLGADHLAQ VQAEAQRIVD AVIG
//
