ID   Q1GZZ9_METFK            Unreviewed;       457 AA.
AC   Q1GZZ9;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   01-MAY-2013, entry version 58.
DE   SubName: Full=Phosphomannomutase;
DE            EC=5.4.2.8;
GN   OrderedLocusNames=Mfla_1921;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I.,
RA   Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR   EMBL; CP000284; ABE50188.1; -; Genomic_DNA.
DR   RefSeq; YP_546029.1; NC_007947.1.
DR   ProteinModelPortal; Q1GZZ9; -.
DR   SMR; Q1GZZ9; 1-457.
DR   STRING; 265072.Mfla_1921; -.
DR   EnsemblBacteria; ABE50188; ABE50188; Mfla_1921.
DR   GeneID; 4001196; -.
DR   KEGG; mfa:Mfla_1921; -.
DR   PATRIC; 32269621; VBIMetFla97085_2031.
DR   eggNOG; COG1109; -.
DR   HOGENOM; HOG000268679; -.
DR   KO; K15778; -.
DR   OMA; CECIVEV; -.
DR   ProtClustDB; CLSK2529592; -.
DR   BioCyc; MFLA265072:GHWJ-1983-MONOMER; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.120.10; -; 3.
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; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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; SSF53738; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein.
SQ   SEQUENCE   457 AA;  49863 MW;  1CE47CA28458CB0B CRC64;
     MTAPKEIFKA YDIRGIVGKT LTPEIVESIG HAIGSEAALR DQKTICIGYD GRLSGPELAA
     ALSRGIRKSG LDVINLGLVA TPMVYFAAYH LQTGSGVMVT GSHNPPEYNG LKMVLAGETL
     SGDTIQRLRA RIDNNDFVHG NGTESSHDIA PAYIERIASD IKLKRPIKLT VDCGNGVPGA
     FAGKLYRALG CEVEELFCEV DGHFPNHHPD PSVPENLKDL IENLLAGQSE IGFAFDGDGD
     RLGVVTKDGS IIYPDRQLLL FAEDVLKRSP KATIIYDVKS TRNLSPWIKQ RGGEPLMWKT
     GHSLVKAKMK ETGAALAGEM SGHIFFKERW YGFDDGLYSG ARLLEILSQF DDPSAVLNAL
     PDSVSTPEQH IHMREGEPHR LISELQASAK FEGANEVITI DGLRVEYSDG FGLMRPSNTT
     PVIVLRFEAD NAEALKRIQE QFRSVILAAA PNAKLPF
//