ID Q7VR96_BLOFL Unreviewed; 548 AA.
AC Q7VR96;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:CAD83393.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:CAD83393.1};
GN Name=pgm {ECO:0000313|EMBL:CAD83393.1};
GN OrderedLocusNames=Bfl326 {ECO:0000313|EMBL:CAD83393.1};
OS Blochmannia floridanus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83393.1, ECO:0000313|Proteomes:UP000002192};
RN [1] {ECO:0000313|EMBL:CAD83393.1, ECO:0000313|Proteomes:UP000002192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; BX248583; CAD83393.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VR96; -.
DR STRING; 203907.Bfl326; -.
DR KEGG; bfl:Bfl326; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_6; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000002192; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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; IPR005852; PGM_a-D-Glc-sp.
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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:CAD83393.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 38..179
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..435
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 548 AA; 62515 MW; 0121B09D902230D5 CRC64;
MQNNLFQVKK SIINETKLID QYYNLSPDPY NNKEHKVFFG TSGHRGSSYQ YSFNEAHVFA
ISQSIVQIRT LYGITGPCYV AKDTHTLSEP AFISVLEVLT ANSINVIIEK NDLYTPTPVI
SNAIINYNRH RYHNNQSKAD GIIVTSSHNP PEDGGIKYSS IFGGPAEIDI TYLIEKYANR
FLLNNLRTVN KITLNHAWRS GYIHPQDLVQ NYVQNLSTII NMKAIQKSGL KIGVDPLSGS
SINCWYDIAQ YYQLNLTVIN SKIDRTFSFM NIDYDGRIRI NCTSELTLSK VLSSSKKFDL
FFINDPDCDR HGIITKGGLI QSNYYFPIVI NYLFHNRDFW KKKILSVGKT NVSSMSIDQV
ANNLNCQLLT TPVGFKWFTQ GLLHSKLGFA GEDSSGASFL DQRCMPWSTD KDGFIMCLIS
AEILAVTDHT LQDHHIQFNK NLNCTFNYNQ TYLVINHSQK KSIINTLFNQ IHMNELVGDP
IIKVENIKPL NKFISMDGLK IVTRNGWIAG RLSGTELVYK IYCESFLSSD HRLKMEQKMI
RCIYQIIN
//
