ID   A4Y0L0_PSEMY            Unreviewed;       863 AA.
AC   A4Y0L0;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   OrderedLocusNames=Pmen_4379 {ECO:0000313|EMBL:ABP87126.1};
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP87126.1};
RN   [1] {ECO:0000313|EMBL:ABP87126.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ymp {ECO:0000313|EMBL:ABP87126.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC         Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC         EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; CP000680; ABP87126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4Y0L0; -.
DR   STRING; 399739.Pmen_4379; -.
DR   KEGG; pmy:Pmen_4379; -.
DR   PATRIC; fig|399739.8.peg.4437; -.
DR   eggNOG; COG1109; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_013562_0_1_6; -.
DR   OrthoDB; 9803322at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:ABP87126.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          413..542
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          559..655
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          660..765
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          775..852
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          339..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  92440 MW;  33BAB1978284366C CRC64;
     MKLFKRTAKE ADTLSSLAPD LPESKRAKPS LGPLLPGLLA ALIGVAAGGA LLWLAQSNSE
     QARQAELAQA IGSSQAAAVQ QALKQLQADS LAAARNPDLL QALQSADSLR IGDAERRLGY
     WDGVVDAHLN RRGEAVQNTS RPAPMNFAGL DMLRRAESGQ QPAVEAYRVG QRWLAYSAVA
     LRLGDNQPAQ GTLLLAVDLQ RLLAALPPLP AELGQVQLVQ QFANTPAQVL LQRGQAGDGA
     AQTFPTGSPY WTISFTPGPG LTGGGVPPLL LGLAALLALG GALIALMLVQ GAMQRRVNSD
     AQQLGQMLKE LSAGKNVKAF SLSLPALNGL AQSLARLPRR NGAEGTSSTP AKGTVAAPTT
     QPAPKPAELV DPLFQDTDIL DIDILDEDQD LLGLEQSPAM TTSQSVPKLP ADIFRAYDIR
     GVVGDTLTAE YAYWIGRAIG SQSLAQGEPK VIVGRDGRLS GPELLQQLVQ GLLDCGCEVT
     DIGMVPTPVV YFAANVLEGR SAVMLTGSHN PPDYNGFKII IAGDTLANEQ IQALKTRLDN
     NDLATGVGSV QQVDVLQRYF KTIRDDIALA KPLKVVVDCG NGAAGVIAPQ LIEALGCSVI
     PLFCEVDGTF PNHHPDPGKP ENLVDLIARV KAENADLGLA FDGDGDRVGV VTNTGNIVYP
     DRLLMLFAKD VVSRNPGADI IFDVKCTRRL TPLISGYGGR PVMWKTGHSL IKKKMKETGA
     LLAGEMSGHI FFKERWYGFD DGIYSAARLL EILSLDKRNA EQVFSAFPSD ISTPEINIQV
     TEQSKFPLIE RLQREGQWGE ANLTSIDGVR VDYPKGWGLI RASNTTPVLV LRFEADTQEE
     LERIQDVFRN QLLKVAPDLQ LPF
//