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Database: UniProt
Entry: A0A1G5NEF4_AFIMA
LinkDB: A0A1G5NEF4_AFIMA
Original site: A0A1G5NEF4_AFIMA 
ID   A0A1G5NEF4_AFIMA        Unreviewed;       543 AA.
AC   A0A1G5NEF4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=SAMN03080610_01807 {ECO:0000313|EMBL:SCZ34980.1};
OS   Afifella marina DSM 2698.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Afifellaceae; Afifella.
OX   NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ34980.1, ECO:0000313|Proteomes:UP000199347};
RN   [1] {ECO:0000313|EMBL:SCZ34980.1, ECO:0000313|Proteomes:UP000199347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ34980.1,
RC   ECO:0000313|Proteomes:UP000199347};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
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DR   EMBL; FMVW01000003; SCZ34980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5NEF4; -.
DR   STRING; 1120955.SAMN03080610_01807; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000199347; Unassembled WGS sequence.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR045244; PGM.
DR   PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199347}.
FT   DOMAIN          14..153
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          185..286
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          295..407
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   543 AA;  57333 MW;  F1CD8C5062728089 CRC64;
     MNIETVSTKP IAGQKPGTSG LRKKTAAFLE PGYLENYIAA IIEGIGGVEG ATMVIGGDGR
     FGNRQAIKTL VRMLGAAGAK HLIIGQNGLL STPAASCVIR KRQATGGFIF SASHNPGGEH
     GDFGLKYNLA NGGPAPENVT SAIYKATQTL SSYKIAELDE IDLSKVATVE HDGLVIEVID
     PVTDYAALME ELFDFDAISG LFAGGFRLAY DAMHAATGPY AKAILEGRLG AAVGTVRNGE
     PLPDFGGLHP DPNPVHAKAL FDLMAAPEAP DMGAASDGDG DRNLVLGPGL PVSPSDSIAI
     LAANAHLAPG YKRGLAGVAR SMPTSRALDR VAEELGISLY ETPTGWKFFG NLLDAGKITM
     CGEESAGAGS DHVREKDGLW AVLLWLNILA VRRQSIPEIV REHWARFGRN YYTRHDYEAI
     ETERAETLMS ELTARLGSLP GEKAGSLTIE GADEFAYHDP IDGSLAEHQG IRVLFEGGGR
     AVFRLSGTGT EGATLRVYLE RFEPAGGDHA QEPQQALAEI IAAAGEVAGI EKHTGRTEPD
     VIT
//
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