ID V9UWJ5_9PSED Unreviewed; 453 AA.
AC V9UWJ5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=X970_04990 {ECO:0000313|EMBL:AHC86797.1};
OS Pseudomonas monteilii SB3101.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC86797.1, ECO:0000313|Proteomes:UP000018660};
RN [1] {ECO:0000313|EMBL:AHC86797.1, ECO:0000313|Proteomes:UP000018660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3101 {ECO:0000313|EMBL:AHC86797.1,
RC ECO:0000313|Proteomes:UP000018660};
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA Nielsen J.L.;
RT "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL Submitted (DEC-2013) 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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CP006979; AHC86797.1; -; Genomic_DNA.
DR RefSeq; WP_024086451.1; NC_023076.1.
DR AlphaFoldDB; V9UWJ5; -.
DR KEGG; pmot:X970_04990; -.
DR PATRIC; fig|1435058.3.peg.986; -.
DR HOGENOM; CLU_016950_9_2_6; -.
DR Proteomes; UP000018660; Chromosome.
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:SF1; 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, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 9..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 156..255
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 375..452
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 453 AA; 49615 MW; 2A5402E15B531EB3 CRC64;
MYAPIQTRCF KAYDIRGQVP ADLNDDIAYR IGRALVAELG GKCYVVGRDM RLESPGLSRA
LMKGLTEGGA EVIDIGLCGT EEVYFATSHY QADGGIMVTA SHNPKGYNGM KLVREQSRPI
SGDTGLNDIR QRVEAGNLGT PGITPGVVRE AFDKSAYIDH LLTYVDVSAL KPLKVLADPG
NGAVGPVLEL LKARLPLDIT IINGEPDGNF PNGIPNPLLP ENRDLTRQAV LDTGADMGIA
FDGDFDRCFF FDNQGRFIEG YYVVGLLAEM LLAKNPGSKI IHDPRLTWNT IEQVEAAGGI
AIQSKTGHAF IKERMRAEDA VYGGEMSAHH YFRDFAYCDS GNIPWLLVAE LMSTTGKSLA
QLVDERIAAF PCSGEINYEV ADVKATIENI LAFYLPHNPE VDRTDGISVA FADWRFSLRG
SNTEPLLRLN VESRADSTLV ERRVNEIARL IRS
//
