ID Q9S3V9_BORBO Unreviewed; 392 AA.
AC Q9S3V9;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AAD48058.1};
GN Name=pgm {ECO:0000313|EMBL:AAD48058.1};
OS Bordetella bronchiseptica (Alcaligenes bronchisepticus).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=518 {ECO:0000313|EMBL:AAD48058.1};
RN [1] {ECO:0000313|EMBL:AAD48058.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BB7865 {ECO:0000313|EMBL:AAD48058.1};
RX PubMed=10899872; DOI=10.1128/IAI.68.8.4673-4680.2000;
RA West N.P., Jungnitz H., Fitter J.T., McArthur J.D., Guzman C.A.,
RA Walker M.J.;
RT "Role of phosphoglucomutase of Bordetella bronchiseptica in
RT lipopolysaccharide biosynthesis and virulence.";
RL Infect. Immun. 68:4673-4680(2000).
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; AF171632; AAD48058.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S3V9; -.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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 PRINTS; PR00509; PGMPMM.
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}.
FT DOMAIN 2..53
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 87..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 189..293
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 303..381
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 392 AA; 42125 MW; E4058853D1339B0A CRC64;
MEGGVDTLDI GQVPTPLVYF AAHTQGTGSG VAVTGSHNPP QYNGFKMMMG GQALYGPAVQ
ALRPAMLAPA AAPGTWGERH QLDVVPAYIE RIVSDVKLAR PMKIAVDCGN GVAGALAPQL
FRALGCEVDE LYCEVDGTFP NHHPDPAEPR NLQDLIAHVT STDCELGLAF DGDGDRLGVV
TKSGQIIWPD RQLILFARDV LARCPGATII YDVKCSRHVG VAIEQSGGVP LMWQTGHSLV
KAKLAETGAP LAGEMSGHIF FKERWYGFDD GLYTGARLLE IVSRETDASR PLEALPQALS
TPELKLEMAE GEPHALIAAL QQQGEFASAS RLVTIDGVRA EYPDGFGLAR ASNTTPVVVL
RFEAETEPGL ARIQQEFRQQ LLRLAPQAKL PF
//
