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Database: UniProt/TrEMBL
Entry: L0M4E4_ENTBF
LinkDB: L0M4E4_ENTBF
Original site: L0M4E4_ENTBF 
ID   L0M4E4_ENTBF            Unreviewed;       456 AA.
AC   L0M4E4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00021706};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   OrderedLocusNames=D782_1578 {ECO:0000313|EMBL:AGB77586.1};
OS   Enterobacteriaceae bacterium (strain FGI 57).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB77586.1, ECO:0000313|Proteomes:UP000011002};
RN   [1] {ECO:0000313|EMBL:AGB77586.1, ECO:0000313|Proteomes:UP000011002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI 57 {ECO:0000313|EMBL:AGB77586.1,
RC   ECO:0000313|Proteomes:UP000011002};
RX   PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA   Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA   Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA   Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA   Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA   Currie C.R.;
RT   "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT   associated with leaf-cutter ant fungus gardens.";
RL   Genome Announc. 1:E00238-12(2013).
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; CP003938; AGB77586.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0M4E4; -.
DR   STRING; 693444.D782_1578; -.
DR   KEGG; ebf:D782_1578; -.
DR   PATRIC; fig|693444.3.peg.1520; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_2_6; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000011002; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011002}.
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..372
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          378..454
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   456 AA;  50265 MW;  1E5C14D5D8EAB1C0 CRC64;
     MKTLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT SEALKLALAR
     GLRDAGVDVL DIGLSGTEEI YFATFHLGID GGIEVTASHN PMDYNGMKLV REGARPISGD
     TGLRDVQRLA EANDFPPVDE SQRGSYQKID LRDAYIDHLL QYINVKNLTP LKLVVNSGNG
     AAGPVIDALE ARFKALNVPV TLIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIEHGADM
     GIAFDGDFDR CFLFDETGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA
     GGTPVMSKTG HAFIKERMRK DDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VSELLCLKGK
     TLGELVRDRM AAFPASGEIN SKLAEPATAI ARVEQYFANE ALEIDRTDGI SLAFADWRFN
     LRSSNTEPVV RLNVESRGDT PLMQARTQDI LALLKQ
//
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