ID J3RU33_ECOLX Unreviewed; 456 AA.
AC J3RU33;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00021706};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AFE83475.1};
RN [1] {ECO:0000313|EMBL:AFE83475.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12B {ECO:0000313|EMBL:AFE83475.1};
RX PubMed=22798363; DOI=10.1128/AEM.01259-12;
RA Norman K.N., Strockbine N.A., Bono J.L.;
RT "Association of Nucleotide Polymorphisms within the O-Antigen Gene Cluster
RT of Escherichia coli O26, O45, O103, O111, O121, and O145 with Serogroups
RT and Genetic Subtypes.";
RL Appl. Environ. Microbiol. 78:6689-6703(2012).
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}.
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DR EMBL; JN887682; AFE83475.1; -; Genomic_DNA.
DR AlphaFoldDB; J3RU33; -.
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; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; 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 7..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 153..258
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 263..366
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 378..449
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 456 AA; 51139 MW; B63242913F58B00E CRC64;
MNKITCFKAY DIRGRLGAEL NDEIAYRIGR AYGEFFKPQT VVVGGDARLT SESLKKSLSN
GLCDAGVNVL DLGMCGTEEI YFSTWYLGID GGIEVTASHN PIDYNGMKLV TKGARPISSD
TGLKDIQQLV ESNNFEELNL EKKGNITKYS TRDAYINHLM GYANLQKIKK IKIVVNSGNG
AAGPVIDAIE ECFLRNNIPI QFVKINNTPD GNFPHGIPNP LLPECREDTS SAVIRHSADF
GIAFDGDFDR CFFFDENGQF IEGYYIVGLL AEVFLGKYPN AKIIHDPRLI WNTIDIVESH
GGIPIMTKTG HAYIKQRMRE EDAVYGGEMS AHHYFKDFAY CDSGMIPWIL ICELLSLTNK
KLGELVCGCI NDWPASGEIN CTLDNPRNEI DKLFNRYKDS ALAVDYTDGL TMEFSDWRFN
VRCSNTEPVV RLNVESRNNA ILMQEKTEEI LNFISK
//
