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Database: UniProt
Entry: J7R2I5_ECOLX
LinkDB: J7R2I5_ECOLX
Original site: J7R2I5_ECOLX 
ID   J7R2I5_ECOLX            Unreviewed;       456 AA.
AC   J7R2I5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00021706};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   Name=cpsG {ECO:0000313|EMBL:MXI73847.1};
GN   ORFNames=BTQ06_10445 {ECO:0000313|EMBL:PAU24123.1}, DRW19_18520
GN   {ECO:0000313|EMBL:EAA6665473.1}, DS732_16260
GN   {ECO:0000313|EMBL:AXO07787.1}, GRW05_05980
GN   {ECO:0000313|EMBL:MXI73847.1}, GUC01_16135
GN   {ECO:0000313|EMBL:NAG20545.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:MXI73847.1, ECO:0000313|Proteomes:UP000436141};
RN   [1] {ECO:0000313|EMBL:PAU24123.1, ECO:0000313|Proteomes:UP000218543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STEC 514-2 {ECO:0000313|EMBL:PAU24123.1,
RC   ECO:0000313|Proteomes:UP000218543};
RA   Ferdous M., Moran-Gilad J., Rossen J.W., Gdalevich M.;
RT   "Real-Time Genomic Investigation Underlying the Public Health Response to a
RT   Shiga Toxin-Producing Escherichia Coli O26:H11 Outbreak in a Nursery.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAA6665473.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=559781 {ECO:0000313|EMBL:EAA6665473.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AXO07787.1, ECO:0000313|Proteomes:UP000256244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cq9 {ECO:0000313|Proteomes:UP000256244}, and Cq9
RC   {ECO:0000313|EMBL:AXO07787.1};
RA   Bai L.;
RT   "Complete genome sequencing and genomic characterization of five
RT   Escherichia coli strains co-producing MCR-1 and ESBLs from different
RT   origins in China.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:NAG20545.1, ECO:0000313|Proteomes:UP000475070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A112 {ECO:0000313|EMBL:NAG20545.1,
RC   ECO:0000313|Proteomes:UP000475070};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
RN   [5] {ECO:0000313|EMBL:MXI73847.1, ECO:0000313|Proteomes:UP000436141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10434wD1 {ECO:0000313|EMBL:MXI73847.1,
RC   ECO:0000313|Proteomes:UP000436141};
RA   Subbiah M., Call D.;
RT   "Enteriobacteria Tanzani isolates_10434.";
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
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; CP031546; AXO07787.1; -; Genomic_DNA.
DR   EMBL; AAACEW010000025; EAA6665473.1; -; Genomic_DNA.
DR   EMBL; WUIY01000016; MXI73847.1; -; Genomic_DNA.
DR   EMBL; WXKQ01000011; NAG20545.1; -; Genomic_DNA.
DR   EMBL; MRVZ01000028; PAU24123.1; -; Genomic_DNA.
DR   RefSeq; WP_001356294.1; NZ_WXYX01000002.1.
DR   Proteomes; UP000218543; Unassembled WGS sequence.
DR   Proteomes; UP000256244; Chromosome.
DR   Proteomes; UP000436141; Unassembled WGS sequence.
DR   Proteomes; UP000475070; Unassembled WGS sequence.
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   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, ECO:0000313|EMBL:MXI73847.1};
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          7..131
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..370
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          378..444
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   456 AA;  50463 MW;  0C6D00AEC17DAE8C CRC64;
     MKKLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT SETLKLALAK
     GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN PMDYNGMKLV REGARPISGD
     TGLRDVQRLA EANDFPPVDE TKRGRYQQIN LRDAYVDHLF GYINVKNLTP LKLVINSGNG
     AAGPVVDAIE ARFKALGAPV ELIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIKHGADM
     GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA
     GGTPVMSKTG HAFIKERMRK EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKEK
     TLGELVRDRM VAFPASGEIN SKLAQPAEAI NRVEQHFSRE ALAVDRTDGI SMTFADWRFN
     LRSSNTEPVV RLNVESRGDV PLMEARTRTL LTLLNE
//
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