ID A0A158M8N9_9BORD Unreviewed; 461 AA.
AC A0A158M8N9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:KAK96292.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KAK96292.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KAK96292.1};
GN Name=algC {ECO:0000313|EMBL:KAK96292.1};
GN ORFNames=L497_2162 {ECO:0000313|EMBL:KAK96292.1};
OS Bordetella holmesii CDC-H585-BH.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK96292.1, ECO:0000313|Proteomes:UP000026682};
RN [1] {ECO:0000313|EMBL:KAK96292.1, ECO:0000313|Proteomes:UP000026682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK96292.1,
RC ECO:0000313|Proteomes:UP000026682};
RA Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA Losada L.;
RT "Genome sequence of Bordetella holmseii.";
RL Submitted (MAR-2014) 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}.
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:KAK96292.1}.
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DR EMBL; JFZZ01000043; KAK96292.1; -; Genomic_DNA.
DR RefSeq; WP_005015461.1; NZ_JFZZ01000043.1.
DR AlphaFoldDB; A0A158M8N9; -.
DR STRING; 35814.BBB42_13915; -.
DR GeneID; 56623963; -.
DR PATRIC; fig|1331206.3.peg.970; -.
DR Proteomes; UP000026682; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KAK96292.1};
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 9..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 156..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 258..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 372..445
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 461 AA; 49785 MW; 20CAE20D4BF19EF5 CRC64;
MKNTYPASVF KAYDIRGTVP DLIDAPFARS LGFALAKRAR SCGNTELVVG YDGRLSSPDL
AVALQEGILE GGVNTFDIGC VPTPLVYFAA YSGQLGAGVA ITGSHNPPKY NGFKMMLGGR
ALYGDDVQAL RADMQAPEGL SADRAGTRRT ANIVPEYIKR VVSDITLARP MKIAIDCGNG
VAGAVAPQLF RALGCDVTEL FCEVDGNFPN HHPDSADPHN LQDLIDCLAT TDCEIGLAFD
GDGDRLGVVT KSGQIIWPDR QLILFARDVL QRCPGQTIIY DVKCSRHVGL AVEQAGGKPL
MWQTGHSLVK AKLAETGAPL AGEMSGHIFF KERWYGFDDG LYTGARLLEI ISRESDPSAL
LEALPTAEST PELKLEMEEG QPHALIRELQ AHGRFDDATQ LITIDGVRAE FTDGFGLARA
SNTTPVVVLR FEAENAAALA RIQTLFKREL LRLAPQARLP F
//
