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Database: UniProt
Entry: A0A1H2I3H5_9PSED
LinkDB: A0A1H2I3H5_9PSED
Original site: A0A1H2I3H5_9PSED 
ID   A0A1H2I3H5_9PSED        Unreviewed;       858 AA.
AC   A0A1H2I3H5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   ORFNames=SAMN05216296_3467 {ECO:0000313|EMBL:SDU38619.1};
OS   Pseudomonas pohangensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=364197 {ECO:0000313|EMBL:SDU38619.1, ECO:0000313|Proteomes:UP000243232};
RN   [1] {ECO:0000313|Proteomes:UP000243232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17875 {ECO:0000313|Proteomes:UP000243232};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; LT629785; SDU38619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2I3H5; -.
DR   STRING; 364197.SAMN05216296_3467; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000243232; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF2; PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000243232};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          408..537
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          553..650
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          655..759
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          770..847
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          338..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          287..314
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   858 AA;  92424 MW;  C89EBAA53AF0CA74 CRC64;
     MIKIKSKKAA AANTSELNEP AAPSSASLLL QGLLPGLGVA ACGLLAGLLL IWFGMLQVSR
     QQQIEQMTQA WGGTQASIIQ QALAQLRDNT QRAASNPQLL QALQSNERDQ IAAAESDLVY
     WDGVLDAQLN QLGKAVQNTQ RAAPMNFAAL DLVRRAESGE PPNPEAYKIN EHWVIYTAAP
     IRTAADQPVL GTLLLAVDLQ RLLKLLPEMP ETVGQFQAAQ QFSNGPAQVL YSTGQAAADS
     SIQLASSNPH WKFSFTPGPQ LTDSGASPLI LLLAALLALA GAFLGIRLAL RNARRALEED
     ADQLQQMVRE LASGKLVKSF NLALPALNTL GKSLAQLPQR KADPASQAVT PQARSEKPEM
     ATDSIPGSFD DILDIDIIEE LPDDYEVTEA EVPAAGGDTQ TPDLPSSIFR AYDIRGVIGS
     TLTATTAYWV GRAIGSQSLA QGEPAVVVAR DGRLSGPELS QALIQGLVEC GCRVIDIGMV
     PTPVLYFATN VLDATSGVMV TGSHNPPDYN GFKIVIAGDT LANEDITALH TRIQQGDLAS
     GNGSLEQQDM LDRYFRHIRD DIAIAKNMKV VVDCGNGVAG VIAPRLIEAL GCTVIPLFCE
     VDGNFPNHHP DPGKLENLQD LIARVREEGA DLGLAFDGDG DRVGVVTNTG NMIYPDRLMM
     VFAKDVVSRN PGADVIFDVK CSRRLGALIS SYGGRPVMWK TGHSLIKKKM KETGALLAGE
     MSGHIFFKER WFGFDDGIYS AARLLEILSL ESRDAEKVFG AFPASLSTPE INITVTDENK
     FALIERLQSK GQWGDANLTL LDGVRVDYPK GWGLVRASNT TPVLVLRFEA DTQAELERIQ
     NIFRAQLQQA APELNLSF
//
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