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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//