ID A0A0N1AD33_9PROT Unreviewed; 467 AA.
AC A0A0N1AD33;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KPF49307.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KPF49307.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KPF49307.1};
GN ORFNames=IP80_07230 {ECO:0000313|EMBL:KPF49307.1};
OS beta proteobacterium AAP65.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF49307.1, ECO:0000313|Proteomes:UP000037849};
RN [1] {ECO:0000313|EMBL:KPF49307.1, ECO:0000313|Proteomes:UP000037849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP65 {ECO:0000313|EMBL:KPF49307.1,
RC ECO:0000313|Proteomes:UP000037849};
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 -!- 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:KPF49307.1}.
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DR EMBL; LJHW01000008; KPF49307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1AD33; -.
DR STRING; 1523424.IP80_07230; -.
DR PATRIC; fig|1523424.3.peg.4088; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000037849; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KPF49307.1};
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:UP000037849}.
FT DOMAIN 7..139
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 155..252
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 257..364
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 371..454
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 467 AA; 50262 MW; 17BD17643389FEE7 CRC64;
MHIDPTVFKA YDIRGIVGKN IDETFAEHLG RAFGSEARAA GEKAVAVGRD GRLSGPKLAA
ALVRGLKSTG LDVVDIGMVT TPMLYYVAAT RAAHGCSSGI MVTGSHNPKD YNGFKMVMSG
RAIYGEDIQK LKLRIETETY TTKRGRSAKM DVLAEYTQRI VGDVKLARPM KVVVDSGNGI
PGASAPGILR ALGCEVIDLY SVVDGDFPNH HPDPSKPENL EVLKTVVRAT GAEVGLAFDG
DGDRLGVVTA TGNIIYPDRQ IMLFARDILS RNKGGTIIYD VKCSQRLPVA IKKAGGKPLM
WKTGHSLIKA KLKEIGAPFA GEMSGHLFFG ERWYGFDDAM YTAARLLEIL AKQKNPSAFL
DALPTSFSTP ELNVPCAEGE HHTVVAELLA RVADGRMKFE GGEVGTIDGL RVDFADGFGL
IRASNTTPVL VLRFEGHTDE ALHRIEAQFM AALREVKPDA QVAAAAH
//
