ID J2XKK9_9PSED Unreviewed; 548 AA.
AC J2XKK9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:EJN25200.1};
GN ORFNames=PMI36_01776 {ECO:0000313|EMBL:EJN25200.1};
OS Pseudomonas sp. GM79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144338 {ECO:0000313|EMBL:EJN25200.1, ECO:0000313|Proteomes:UP000007512};
RN [1] {ECO:0000313|EMBL:EJN25200.1, ECO:0000313|Proteomes:UP000007512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM79 {ECO:0000313|EMBL:EJN25200.1,
RC ECO:0000313|Proteomes:UP000007512};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN25200.1}.
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DR EMBL; AKJE01000032; EJN25200.1; -; Genomic_DNA.
DR RefSeq; WP_008069864.1; NZ_AKJE01000032.1.
DR AlphaFoldDB; J2XKK9; -.
DR PATRIC; fig|1144338.3.peg.1750; -.
DR Proteomes; UP000007512; 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; 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 Pfam; PF00408; PGM_PMM_IV; 1.
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 40..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 323..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 493..538
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 548 AA; 58946 MW; 9DF15A5CB9D8BA36 CRC64;
MTLSPFAGKP APAELLVDIP RLVTAYYTGQ PDAAISTQRV AFGTSGHRGS SFDLSFNEWH
VLAISQAICL YREAQGIDGP LFVGIDTHAL STPAGASALE VLAANGVTVM IAEGDEYTPT
PAISHAILCY NRGRTSGLAD GIVITPSHNP PQSGGYKYNP TNGGPADTHI TKWIEAKANE
LLAAKLAGVK RISYEQALKA STTHRHDYLN TYVADLINVI DFDAIREAKL RLGVDPLGGA
GVRYWSAIAE HYRLDLEVVN KQVDATFRFM TVDWDGQIRM DPSSSHAMQG LIGLKERFDV
AFACDPDHDR HGIVTPSGGL LAPNNYLAVS IDYLFQNRPL WRADAAVGKT VVSSGLIDRV
AKRLGRRLYE VPVGFKWFAD GLFDGSLGFG GEESAGASFL RKDGSVWCTD KDGLIPALLA
AEMTARTGRD PSQAYRALTD ELGEPFSVRV DAKANPEQKA LLSKLSPDQV TSTQLAGEAI
QSILSHAPGN DQAIGGLKVM TENGWFAARP SGTEDIYKIY AESFVSDDHL KQLVAEAQTL
VDGAISAK
//
