ID Q9RIF4_YEREN Unreviewed; 146 AA.
AC Q9RIF4;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00021706};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
DE Flags: Fragment;
GN Name=manB {ECO:0000313|EMBL:CAB58200.1};
OS Yersinia enterocolitica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630 {ECO:0000313|EMBL:CAB58200.1};
RN [1] {ECO:0000313|EMBL:CAB58200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=25936 {ECO:0000313|EMBL:CAB58200.1};
RX PubMed=10570195; DOI=10.1073/pnas.96.24.14043;
RA Achtman M., Zurth K., Morelli G., Torrea G., Guiyoule A., Carniel E.;
RT "Yersinia pestis, the cause of plague, is a recently emerged clone of
RT Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14043-14048(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ270449; CAB58200.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RIF4; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:CAB58200.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 2..52
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 78..145
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB58200.1"
FT NON_TER 146
FT /evidence="ECO:0000313|EMBL:CAB58200.1"
SQ SEQUENCE 146 AA; 16075 MW; 50F307C95943C798 CRC64;
GTEEIYFSTF HLDVDGGIEV TASHNPIDYN GMKLVRKNAC PISGDTGLRN IQHLAEINKF
PPVEPSMRGS YDKISIIDDY IDHLMGYINP SLFKPLRLVV NSGNGAAGHV IDALEKRFTA
LDIPITLIKI HNEPDGTFPH GIPNPL
//
