ID W1DY12_KLEPN Unreviewed; 306 AA.
AC W1DY12;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CDL13014.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CDL13014.1};
OS Klebsiella pneumoniae IS43.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL13014.1, ECO:0000313|Proteomes:UP000019183};
RN [1] {ECO:0000313|EMBL:CDL13014.1, ECO:0000313|Proteomes:UP000019183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS43 {ECO:0000313|EMBL:CDL13014.1,
RC ECO:0000313|Proteomes:UP000019183};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:CDL13014.1}.
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DR EMBL; CBWK010000876; CDL13014.1; -; Genomic_DNA.
DR AlphaFoldDB; W1DY12; -.
DR Proteomes; UP000019183; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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; 2.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:CDL13014.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 3..107
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 114..220
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 229..305
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 306 AA; 33973 MW; BC8804FB13883B3E CRC64;
MLKEYVDHLM GYVDLANFTR PLKLVVNSGN GAAGHVIDEV EKRFAAAGAP VTFIKVHHQP
DGHFPNGIPN PLLPECRQDT ADAVRVHQAD MGIAFDGDFD RCFLFDDEAS FIEGYYIVGL
LAEAFLQKQP GAKIIHDPRL TWNTVDIVTR SGGQPVMSKT GHAFIKERMR QEDAIYGGEM
SAHHYFRDFA YCDSGMIPWL LVAELLCLKN SSLKSLVADR QAAFPASGEI NRKLGNAAEA
IARIRAQYEP AAAHIDTTDG ISIEYPEWRF NLRTSNTEPV VRLNVESRAD TALMNAKTEE
ILALLK
//
