ID F6A9G8_PSEF1 Unreviewed; 857 AA.
AC F6A9G8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN OrderedLocusNames=Psefu_4306 {ECO:0000313|EMBL:AEF24258.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF24258.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF24258.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) 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; CP002727; AEF24258.1; -; Genomic_DNA.
DR AlphaFoldDB; F6A9G8; -.
DR STRING; 743720.Psefu_4306; -.
DR KEGG; pfv:Psefu_4306; -.
DR eggNOG; COG1109; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_013562_0_1_6; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000000686; Chromosome.
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: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};
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:UP000000686};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..536
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 553..649
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 654..761
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 769..843
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 91657 MW; 9E66FF85007674CD CRC64;
MKGFKRAPKE ERPGDSQPAP RSQAKASADL LPGVIAAALG VALAGAILWF AAVSPAQQVQ
QQQLSQAWGS GQAASLQQAL KQLSADTLAA ARNPALAQAL QSGDDAQVRN AENGLRYWNG
VVDAQLNLPG QAVPDSSRAA PMNFAALDLL RRLEAGQAPA VEAYKVGERW LAYSVAPVRQ
DDKQPMVGTL LLAVDLNRLL GNLPPLPADV GQIQLVQRFD AGAAQVLAQR GQAEGTPQAF
ATGNPHWTLN FTPAAGLGNT GLSPALLGLA LLVALAGALI GLLLVNRGLQ QRLARDVAQL
SELVKELSAG KAVKAFSLSL PALNNLAQNL SRLPRRAQYP VATRPEPAAS EAPSNRVAAK
PADFVNPLFQ DTDILDIDIL DDDQDLLGLE QTPIMSAPQA PKLPADIFRA YDIRGVVGAG
LTPETAYWIG RAIGSQSLAE GEPNVAVGRD GRLSGPSLVE QLIQGVADSG CHVSDVGMVP
TPVVYFAAHV LAGKTAVMLT GSHNPPDYNG FKIVIAGDTL ANEQIQALKN RIDNNDLSSG
EGSVERVDLL PRYLEQIRSD IAMAKPLRVV VDCGNGAAGV IAPQLIEALG CTVIPLYCEV
DGNFPNHHPD PGKPENLVDL IAKVKEENAD VGLAFDGDGD RVGVVTNTGT IVYPDRLLML
FAKDVVSRNP GADIIFDVKC TRRLTPLISG YGGRPVMWKT GHSLIKKKMK ETGALLAGEM
SGHVFFKERW FGFDDGIYAA ARLLEILSQD KRTAEQVFAA FPNDVSTPEI NVQVTEQTKF
PIIERLQREG QWGEGSVTNL DGVRVDYPKG WGLVRASNTT PVLVLRFEAE SQAELERIQE
LFRSQMHRVA PDVQLPF
//
