ID A0A1K1MUR3_9GAMM Unreviewed; 547 AA.
AC A0A1K1MUR3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SFW25710.1};
GN ORFNames=SAMN02800691_0582 {ECO:0000313|EMBL:SFW25710.1};
OS Luteibacter sp. UNCMF366Tsu5.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1502758 {ECO:0000313|EMBL:SFW25710.1, ECO:0000313|Proteomes:UP000182005};
RN [1] {ECO:0000313|EMBL:SFW25710.1, ECO:0000313|Proteomes:UP000182005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCMF366Tsu5.1 {ECO:0000313|EMBL:SFW25710.1,
RC ECO:0000313|Proteomes:UP000182005};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FPIS01000001; SFW25710.1; -; Genomic_DNA.
DR RefSeq; WP_072321009.1; NZ_FPIS01000001.1.
DR AlphaFoldDB; A0A1K1MUR3; -.
DR STRING; 1502758.SAMN02800691_0582; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000182005; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 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 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:UP000182005}.
FT DOMAIN 42..183
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 547 AA; 58272 MW; 40E4C33049B5F932 CRC64;
MSAKISPLAG KPATESQPVD VAALLAAYHD LTPDPSVPEQ RVAFGTSGHR GSSFDRSFNE
WHVLAVVQAI CEYRVRSGVD GPLFVGIDTH ALSGPAFEST LEVLAANDVQ TQVSAGGEYT
PTPAVSHAIL TYNRGREHGL ADGIVITPSH NPPESGGIKY NPPHGGPADT DATGWIAARA
NALMEGGLRD VKRMPFAQAI KASNTHEYDF LQRYVGDLGD VLDLEIIRAQ GVRMGVDPLG
GAGVHYWSAI GERYGLDLTV VSETVDPTFS FMSLDWDGRV RMDPSSSYAM QRLIGLKDRF
EVAFACDTDH DRHGVVAPST GLMQANHYLA TAAWYLFQNR PGWRADAAIG KTAVTTALID
RIAKHLGRPL REVPVGFKYF VSGLYDGSLG FGCEESAGAS FLTKNGSAWS TDKDGIAAAL
LAGEMTARMG KDPGQIYGDV TALLGDPANA RIDAPANHAQ KAKLSKLAPT QVTSTILAGD
PIVDVTNQAG GQGIGGIKVV SDHGWFAARP SGTEDIYKVY GESFRGKEHL QTVLEEAQAM
VDRALAD
//
