ID J2YM90_9PSED Unreviewed; 545 AA.
AC J2YM90;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:EJN37545.1};
GN ORFNames=PMI38_02970 {ECO:0000313|EMBL:EJN37545.1};
OS Pseudomonas sp. GM84.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144340 {ECO:0000313|EMBL:EJN37545.1, ECO:0000313|Proteomes:UP000007504};
RN [1] {ECO:0000313|EMBL:EJN37545.1, ECO:0000313|Proteomes:UP000007504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM84 {ECO:0000313|EMBL:EJN37545.1,
RC ECO:0000313|Proteomes:UP000007504};
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:EJN37545.1}.
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DR EMBL; AKJC01000170; EJN37545.1; -; Genomic_DNA.
DR RefSeq; WP_008095207.1; NZ_AKJC01000170.1.
DR AlphaFoldDB; J2YM90; -.
DR PATRIC; fig|1144340.3.peg.2801; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000007504; 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 322..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 492..535
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 545 AA; 58623 MW; A3DC3AC6387CFBD1 CRC64;
MTLSPLAGKP APASVLVDIP RLLTAYYTGR PDAAVAAQRV AFGTSGHRGS SFDLSFNESH
VLAITQAICL YRQEKGIDGP LFIGADTHAL SAPAAASALE VLAANGVQVM LSKDDEYTPT
PAVSHAILCY NRGRAQGLAD GIVITPSHNP PQSGGFKYNP PNGGPADSDV TKWIEAKANE
LLAADLAGVK RMDYAQALQA PTTQRHDYIE HYVADLENVI DFDVIRAANL RLGVDPLGGA
GVRYWSAIAE RYQLNLEVVN TEVDPTFRFM TVDWDGQIRM DPSSPYAMQG LIGLRERFDV
AFACDPDHDR HGIVTADGLL QPNNYLAVAI DYLYRHRPQW RSDAAVGKTV VSSGMIDRVT
ERLGRELYEV PVGFKFFAQG LFDGSLGFGG EESAGASFLR KDGSVWATDK DGLIPALLAA
EMTARTGRNP SQAYDDLTQA LGKPFATRVE AKADARQKAL LSKLAPEQVK STELAGEPIV
QILSHAPGNG QAIGGLKVMT ANGWFAARPS GTEDIYKIYA ESFVDEAHLQ RLVAEAQVLV
DAAIA
//
