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Database: UniProt
Entry: K7YQ89_BDEBC
LinkDB: K7YQ89_BDEBC
Original site: K7YQ89_BDEBC 
ID   K7YQ89_BDEBC            Unreviewed;       455 AA.
AC   K7YQ89;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN   Name=pmm {ECO:0000313|EMBL:AFX99727.1};
GN   ORFNames=Bdt_0014 {ECO:0000313|EMBL:AFX99727.1};
OS   Bdellovibrio bacteriovorus str. Tiberius.
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFX99727.1, ECO:0000313|Proteomes:UP000010074};
RN   [1] {ECO:0000313|EMBL:AFX99727.1, ECO:0000313|Proteomes:UP000010074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tiberius {ECO:0000313|EMBL:AFX99727.1,
RC   ECO:0000313|Proteomes:UP000010074};
RX   PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA   Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA   Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA   Sockett R.E.;
RT   "Genome analysis of a simultaneously predatory and prey-independent, novel
RT   Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT   predictions of both ancient and recent lateral gene transfer from diverse
RT   bacteria.";
RL   BMC Genomics 13:670-670(2012).
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; CP002930; AFX99727.1; -; Genomic_DNA.
DR   RefSeq; WP_015089223.1; NC_019567.1.
DR   AlphaFoldDB; K7YQ89; -.
DR   STRING; 1069642.Bdt_0014; -.
DR   KEGG; bbat:Bdt_0014; -.
DR   PATRIC; fig|1069642.3.peg.14; -.
DR   HOGENOM; CLU_016950_9_1_7; -.
DR   Proteomes; UP000010074; 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: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};
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..138
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..251
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          256..365
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          371..451
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   455 AA;  49968 MW;  BC8929B6CD212D47 CRC64;
     MFQPVIFREY DIRGVYNGQF DDNFAYLLGR AYVVYMKQNK NITNPTVALG CDARESSPAI
     IKNLAKGLMD SGANVIHLGL VTTPVCYFAT FELKVDGAVQ VTGSHNPPEY NGFKISVGKG
     TIFGVEIQKL LHIIQKGEFI DGQGSEESFD IKPMYYARYA KEFGHIKDTK VVLDCGNGAG
     GSVVRGLFEA CGLKPTILFE QPDGTFPNHH PDPTVEENLV DLKAQVLKEG AVAGIGFDGD
     ADRIGVVDHT GRMVYGDELM VIISRAILAE QKGAKIIGDV KCSDRLYHDV AKHGGQPIMW
     KTGHSLVKEK IKVEKAPFGG EMSGHVFFAD RNHGYDDAPY AALRLVEILA KTGKTIPQLL
     EGLPPSFNTP EIRIDTTEEK KVLIVEKMIE AFPAKEGADY KVDFTDGIRL SFADGWALCR
     SSNTQPVVVV RYESSSQAGL DAIRNRVEAI VNKYL
//
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