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Database: UniProt
Entry: A0A0U3AX11_9ALTE
LinkDB: A0A0U3AX11_9ALTE
Original site: A0A0U3AX11_9ALTE 
ID   A0A0U3AX11_9ALTE        Unreviewed;       547 AA.
AC   A0A0U3AX11;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ALS98639.1};
GN   ORFNames=AT746_10410 {ECO:0000313|EMBL:ALS98639.1};
OS   Lacimicrobium alkaliphilum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Lacimicrobium.
OX   NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS98639.1, ECO:0000313|Proteomes:UP000068447};
RN   [1] {ECO:0000313|EMBL:ALS98639.1, ECO:0000313|Proteomes:UP000068447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YelD216 {ECO:0000313|EMBL:ALS98639.1,
RC   ECO:0000313|Proteomes:UP000068447};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; CP013650; ALS98639.1; -; Genomic_DNA.
DR   RefSeq; WP_062480049.1; NZ_CP013650.1.
DR   AlphaFoldDB; A0A0U3AX11; -.
DR   STRING; 1526571.AT746_10410; -.
DR   KEGG; lal:AT746_10410; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000068447; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
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   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:UP000068447}.
FT   DOMAIN          41..178
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..315
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          322..437
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          493..541
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   547 AA;  59445 MW;  F439D5EA87FB6350 CRC64;
     MALDPRAGQL AGPQDLVNIP RLVAAYYSNQ PDKTEPAHAV AFGTSGHRGS SLEYTFNDWH
     IAAICQALAE YRQTNNISGP LFMGMDTHAL SEPAFITALE VLCANDVTVV VEVERGYTPT
     PAISHAILNY NLGRETGLGD GVVITPSHNP PQDGGFKYNP PHGGPADTQV TDAIQIRAND
     LIAAELNGVK RMTFAAALRS GLVHEKDFAK SYIDELDQVI DLQAISSAKL KLGTDPLGGA
     GLHYWHRIAE QYKLDIEVVN PYQDPTFRFM HLDKDGKIRM DCSSASAMAG LIALKDRFDL
     AFGNDADFDR HGIVCRGSGL MNPNHYLAVA IDYLYRHRSQ WHKQMKIGKT LVSSAMIDRV
     AADLGRELAE MPVGFKWFVP YLLEGSMGFA GEESAGGIFL RRDGSTWATD KDGIIMCLLA
     AEILAVTGKD PAEHYDLLAL KFGQPSYKRL DVSASASQKI KLNKMTAEVI TSTTLAGEAI
     SQVLTRAPGN DAAIGGLKVS TESGWFAARP SGTEAVYKIY AESFKDEKHL KLLLNEAQDL
     IAGVFNS
//
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