ID U3P6X0_LEIXC Unreviewed; 559 AA.
AC U3P6X0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=O159_04760 {ECO:0000313|EMBL:AGW40672.1};
OS Leifsonia xyli subsp. cynodontis DSM 46306.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1389489 {ECO:0000313|EMBL:AGW40672.1, ECO:0000313|Proteomes:UP000016743};
RN [1] {ECO:0000313|EMBL:AGW40672.1, ECO:0000313|Proteomes:UP000016743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46306 {ECO:0000313|EMBL:AGW40672.1};
RX PubMed=24201198;
RA Monteiro-Vitorello C.B., Zerillo M.M., Van Sluys M.A., Camargo L.E.,
RA Kitajima J.P.;
RT "Complete Genome Sequence of Leifsonia xyli subsp. cynodontis Strain
RT DSM46306, a Gram-Positive Bacterial Pathogen of Grasses.";
RL Genome Announc. 1:e00915-13(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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; CP006734; AGW40672.1; -; Genomic_DNA.
DR RefSeq; WP_021754113.1; NC_022438.1.
DR AlphaFoldDB; U3P6X0; -.
DR STRING; 1389489.O159_04760; -.
DR KEGG; lxy:O159_04760; -.
DR PATRIC; fig|1389489.3.peg.458; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_2_11; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000016743; 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; cd05799; PGM2; 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; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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 53..192
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 217..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 332..443
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 485..543
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 559 AA; 58294 MW; A483A93A3B7FE5F4 CRC64;
MSDTAQLLAD ARVWLEQDPD PETHRELTAL LADAESGSAG AIADLRSRFG ARLAFGTAGL
RGEIAAGPNR MNRVLVAQAA AGFAHWLMEN AEDGTPSVVI GYDGRKNSDV FARDTAELMA
GAGVCAILLP RLLPTPVLAF AIRHLGTSAG VMVTASHNPR NDNGYKVYLG GKSHGSQIVS
PTDAEIAAHI LEVARGSVAE LPRSEQYEVA GEEVERDYIA ATAAVASTSA PRDAVSFAYT
AMHGVGWRTA REVFARAGFA EPAVVTAQRD PDPAFPTVAF PNPEEPGAMD LAFATAREAG
ADLVIANDPD ADRLAVAIPD PAAAEGYRRL SGNEVGALLG WRAAELAAGE GGALACSIVS
SPALAAVAEA YRLGFANTLT GFKWVSRAPG LIFGYEEALG YLVNPQTIRD KDGISAATAL
LDLASSLAAE GRTIADQLDA FAERFGFFAS EQISLRVSDV SRIGEIMAAL RATPPSHLGA
VPVSRIDDLS DGLGGLPPSD VLRILLADGS RVMVRPSGTE PKLKIYIDAS SDEGALAERR
STAAARVAAL AEAMRALTA
//
