ID   C7R7U6_KANKD            Unreviewed;       806 AA.
AC   C7R7U6;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   OrderedLocusNames=Kkor_2220 {ECO:0000313|EMBL:ACV27629.1};
OS   Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV27629.1, ECO:0000313|Proteomes:UP000001231};
RN   [1] {ECO:0000313|EMBL:ACV27629.1, ECO:0000313|Proteomes:UP000001231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC   {ECO:0000313|Proteomes:UP000001231};
RX   PubMed=21304661; DOI=10.4056/sigs.36635;
RA   Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA   Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL   Stand. Genomic Sci. 1:226-233(2009).
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; CP001707; ACV27629.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7R7U6; -.
DR   STRING; 523791.Kkor_2220; -.
DR   KEGG; kko:Kkor_2220; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_013562_0_1_6; -.
DR   InParanoid; C7R7U6; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000001231; Chromosome.
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:ACV27629.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000001231};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          356..486
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          501..598
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          603..710
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          718..795
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          300..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..318
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  88715 MW;  EF67CDFBDE54467F CRC64;
     MGKGKSLVSF FLLPLIIGLA LLCVVGAVLY YLGIQQPLEA QAKQLIGSQI EERADLIEQK
     INQIQSTIAV ASQTGDETDE VQLVRDLKAS IPQADQVQFF SPEDFQVNLD NRPIVTHVVV
     DLLRKSMAGE EVSPELILNK GQVDYVAFVH KLNDQRALML TVQPSQMVSL LGAADPGTYF
     ELRQSFAESH HTIAAVGTNP GAGNPLVVSP AFGANWTIAF WQGSGNFLAT AGLLPILLML
     GAVIALLIAA LMPMLSLQRL LNKDARDFIQ GIDDQHMPNH FSLKFFNDMA SSYRRLAGLQ
     EPAEKEQDDE EVVDSGLNVE DDTGEKQESA RPKKQAPLNN GNYDLETLSH EISADIFREY
     DVRGRVDKDF DEGVVYALGL AIGSEAYARG EQNVVVARDG RLSSPELHEA LKLGLIESGR
     NVIDLGMVPT PLLYFATHKL DTHSGVMLTG SHNPSNHNGL KVVLAGETLH GKDVKSLYTR
     IREQDFLSGH GQVTEHKIEQ EYLEEVASNV KVDKPLKLVI DSGNGVTGNI APRLFQALGC
     DVIGLHTTID GNFPNHHPDP NHAKNLQDVI AMVLQEKADV GLAFDGDGDR LGVIDNQGNV
     IWTDRLMMLF AMDVLSRKNG AEIIYDVKCT RHLPEIIKKH GGHPIIWKTG HSLMKAKMQE
     TGAQLGGEGS GHIYFKERWY GFDDALYAAA RLLEILGKDP RSLAEVFEPL PQSLETEEIN
     VPVADKIKFK LIEVLIKKAQ FGEGRISTID GIRVEYPDRW LLARASNTTP SIVVKFEADS
     SDALEQVKTL LREQLLAIAP KLKINF
//