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Database: UniProt
Entry: N9W0G6_9SPHN
LinkDB: N9W0G6_9SPHN
Original site: N9W0G6_9SPHN 
ID   N9W0G6_9SPHN            Unreviewed;       456 AA.
AC   N9W0G6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ENY80992.1};
GN   ORFNames=EBMC1_11680 {ECO:0000313|EMBL:ENY80992.1};
OS   Sphingopyxis sp. MC1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY80992.1, ECO:0000313|Proteomes:UP000013072};
RN   [1] {ECO:0000313|EMBL:ENY80992.1, ECO:0000313|Proteomes:UP000013072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|EMBL:ENY80992.1,
RC   ECO:0000313|Proteomes:UP000013072};
RA   Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT   "Differential expression analysis of membrane associated proteins from
RT   triclosan-degrading sphingopyxis.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENY80992.1}.
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DR   EMBL; AOUN01000008; ENY80992.1; -; Genomic_DNA.
DR   AlphaFoldDB; N9W0G6; -.
DR   PATRIC; fig|1174684.3.peg.2352; -.
DR   eggNOG; COG1109; Bacteria.
DR   Proteomes; UP000013072; Unassembled WGS sequence.
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, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013072}.
FT   DOMAIN          3..130
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          150..246
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          250..357
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          366..443
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   456 AA;  48362 MW;  D39FF27A32E7B3BE CRC64;
     MLREYDIRGV VGDTLSDADA HAIGRSFATL IARAGGKRVA VGYDGRLSSP MLADALIAGI
     NAAGIDALNV GLGPTPMLYY AASTEDVDGG IQITGSHNPP DYNGFKMVFQ GRPFFGADIQ
     RIGEMAAAGD WEAVNPGGEG TAQSIDIVDA YVDRLVQGFA GGAFRIGWDA GNGAAGTVIE
     KLTARLPGEH HLLYTDIDGH FPNHHPDPTE EKNLADLKAL VAAKKLDFGV AFDGDGDRIG
     AIDGEGRVIW GDQLLQIYAA AVLKERPGAT VIADVKASQA LFDRVAELGG KPLMWKTGHS
     LIKAKMKETG SPLAGEMSGH IFFADHYYGY DDAPYAAVRL IEAATKLGKS VTQLRGEMPA
     MVNTPELRFQ VDEVRKFAIV DEVLARLTAA GATVDRTDGA RVLTDDGWWL LRASNTQDVL
     VARAEAKDEA ALARLMAAID DQLAASGVVR GPQAAH
//
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