ID   E6VPC2_RHOPX            Unreviewed;       498 AA.
AC   E6VPC2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ADU43671.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ADU43671.1};
GN   OrderedLocusNames=Rpdx1_2063 {ECO:0000313|EMBL:ADU43671.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU43671.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) 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}.
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DR   EMBL; CP002418; ADU43671.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VPC2; -.
DR   STRING; 652103.Rpdx1_2063; -.
DR   KEGG; rpx:Rpdx1_2063; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_5; -.
DR   OrthoDB; 9803322at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS10115-MONOMER; -.
DR   Proteomes; UP000001402; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADU43671.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          26..154
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          175..271
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          277..388
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          413..485
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   498 AA;  54483 MW;  DE3677109A537CFF CRC64;
     MFPTPQPLLT ANTYAYESEP MVKPTGFREY DARWLFGQEI NLMGVQALGM GLGTLIAELG
     RPQEIVTGHD FRSYSASIKY ALIAGLMASG CKVHDIGLAV TPMAYYAQFD LDVPCVAMVT
     ASHNDNGWTG VKMGANRPLT FGPDEMNRLK QIVLGAAFKT GSGSYVFHEN YPARYIADLT
     KHARLKRKLK VVVACGNGTA GAFAPQVMEA IGCEVIPLDT ELDHTFPKYN PNPEDMEMLH
     AIRDAVLQHN ADLGLGFDGD GDRCGVVDDT GEEIFADKVG VMLARDMSAI HPNARFVVDV
     KSTGLFATDP VLQRQGARTE YWKTGHSYMK RRTNESNALA GFEKSGHFFF NAPLGRGYDD
     GLVSAIAICE MLDRAPDKSM SQLKGALPKT WSSPTMSPHC ADEVKYRVID EVVKHFEAAQ
     ANGDLVAGQK IRDLVTVNGV RVTCADGSWG LVRASSNKPE LVVVVESPVS EQRMHDMFEA
     VNLVLRQHPE VGAYNQTI
//