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Database: UniProt
Entry: A0A0G0NVU2_9BACT
LinkDB: A0A0G0NVU2_9BACT
Original site: A0A0G0NVU2_9BACT 
ID   A0A0G0NVU2_9BACT        Unreviewed;       462 AA.
AC   A0A0G0NVU2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   ORFNames=UT11_C0015G0011 {ECO:0000313|EMBL:KKQ90004.1};
OS   Berkelbacteria bacterium GW2011_GWA2_38_9.
OC   Bacteria; Candidatus Berkelbacteria.
OX   NCBI_TaxID=1618334 {ECO:0000313|EMBL:KKQ90004.1, ECO:0000313|Proteomes:UP000033934};
RN   [1] {ECO:0000313|EMBL:KKQ90004.1, ECO:0000313|Proteomes:UP000033934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKQ90004.1}.
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DR   EMBL; LBVO01000015; KKQ90004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0NVU2; -.
DR   PATRIC; fig|1618334.3.peg.274; -.
DR   Proteomes; UP000033934; Unassembled WGS sequence.
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          6..143
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          160..260
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          264..375
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          381..454
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   462 AA;  51511 MW;  1C6646D826BA7DE9 CRC64;
     MNIDQSIFKA YDIRGTVPDQ INPKVAEQIG RAFAGWLSKV RANGRSPVLK VIVGRDVRTH
     SPEIAGALIR GIASQSIDVV DVGLITTPML YFIDASAGFD GGVSVTASHN PAEYNGFKIV
     REKAIAISGD SGIKEIGQMA TSQNFPDLVK GQVTQEDFTD RYIDHLQTFI NFKDLKPAKI
     VVNPNFGVGS NILKKLANIV PGEFVYLNSE LDGSFPKGKP DPLLPVNRTE ISELIKSTGA
     DFGVSWDADG DRVYFLDQNG EFIDGYFTTA VLAEAMLKSH PGSKIIYDPR LTWATIDTVN
     RNGGIPIVCK PGHSFFKQRM RSEDALFAGE MSGHYYFRDN FYADDGMLAF LIIWDLYTKK
     NCQYSDLVKD LKAKYITAGQ EFNFEVQDSR SVLAQIEENY TDSQKLEIDG LTIEYPDWRF
     NLRPSNTEPL IRLNIEAKSQ ITFNQKLQEI TDLIKQLGGV EK
//
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