ID   A0A0M3TB59_9SPHN        Unreviewed;       471 AA.
AC   A0A0M3TB59;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ALE17946.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ALE17946.1};
GN   ORFNames=AMC99_02675 {ECO:0000313|EMBL:ALE17946.1};
OS   Altererythrobacter epoxidivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE17946.1, ECO:0000313|Proteomes:UP000057938};
RN   [1] {ECO:0000313|EMBL:ALE17946.1, ECO:0000313|Proteomes:UP000057938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE17946.1,
RC   ECO:0000313|Proteomes:UP000057938};
RA   Li Z., Cheng H., Huo Y., Xu X.;
RT   "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT   Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; CP012669; ALE17946.1; -; Genomic_DNA.
DR   RefSeq; WP_061927190.1; NZ_CP012669.1.
DR   AlphaFoldDB; A0A0M3TB59; -.
DR   STRING; 361183.AMC99_02675; -.
DR   KEGG; aep:AMC99_02675; -.
DR   PATRIC; fig|361183.4.peg.2628; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000057938; Chromosome.
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:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; 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:ALE17946.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057938}.
FT   DOMAIN          10..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..257
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          261..368
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          377..458
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   471 AA;  50438 MW;  7DBDE48A8F8C1968 CRC64;
     MKHQFDSTVL REYDIRGIIG ETLGPDDARA IGRSFATLLR RAGGSKVAVG YDGRVSSPML
     EHALVEGLTA SGCDVVRVGM GPTPMLYYAE ASAEDVHGGI QITGSHNPAN YNGFKMVFQG
     RPFFGEDIQT IGTMSAAGDW SDGTGDVESR DILGEYVERL LEGLAGIDAD ALVSLRVGWD
     AGNGAAGPAL EALAARLPGE HHLLYTEVDG NFPNHHPDPT VEANLADLKA LVADKQLDFG
     VAFDGDGDRI GAIDGEGRVI WGDQLLMIYA EDLLRTRKDA TIIADVKASR ALFDHVSACG
     GKPLMWKTGH SLIKSKMKET GSPLAGEMSG HVFFADTYYG FDDALYAGVR LIAASARLGK
     SVTQLRGDMP DMLNTPEMRF QVDESRKFAA IDEVSARLAD NPGPGVEDVN ATDGVRVTTA
     DGWWLLRASN TQDVLVARAE SDTKDGLDRL MAQIDEQLAL SGLERGESVG H
//