ID A0A0N1AJE0_9SPHN Unreviewed; 543 AA.
AC A0A0N1AJE0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=IP65_12750 {ECO:0000313|EMBL:KPF53859.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF53859.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF53859.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF53859.1,
RC ECO:0000313|Proteomes:UP000037880};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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, 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:KPF53859.1}.
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DR EMBL; LJHO01000005; KPF53859.1; -; Genomic_DNA.
DR RefSeq; WP_022677374.1; NZ_LJHO01000005.1.
DR AlphaFoldDB; A0A0N1AJE0; -.
DR STRING; 1523413.IP65_12750; -.
DR PATRIC; fig|1523413.3.peg.3624; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000037880; Unassembled WGS sequence.
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 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; IPR016066; A-D-PHexomutase_CS.
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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037880}.
FT DOMAIN 14..151
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..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; 57250 MW; 97DB116611248F76 CRC64;
MTITTHQTTP YAGQKPGTSG LRKKVRVFAQ PNYAENFIQA VFDVVERAPG STLVIGGDGR
YHNRTVIQQA IRMAAANGYG QVLVGQGGIL STPAASNVIR RYKASGGLIL SASHNPGGPD
EDFGIKYNIA NGGPAPEGVT EAIYARTQTI DRWLAVDAAD IDLDTCGSVD VGGCQVSVID
PVADYADLME TLFDFAAIRA AVADGLTMAF DAMHAVTGPY ATEILEKRLG FAPGTVRHGV
PLEDFGGHHP DPNMVHAKAL FDAMFGPDAP DFGAASDGDG DRNLIVGKGR FITPSDSLAM
LAANAHLAPG YARGLAGIAR SMPTSAAADR VAEALGIPAY ETPTGWKFFG NLLDAGMATI
CGEESAGTGS DHVREKDGLW AVLLWLNILA VRKISVDELA REHWAKYGRN YYARHDYEGL
PTEQADALMA ALNGKLASLP GQSFGPLTVA TADSFSYLDP VDGSTSANQG LRVLFEGGSR
IVFRLSGTGT EGATLRVYLE RYEPADGYLD RETSDMLADL IAAADAVAGI VAHTGRTAPD
VIT
//
