ID A0A127B4Y3_9BACT Unreviewed; 582 AA.
AC A0A127B4Y3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AMM52501.1};
GN ORFNames=TH61_16755 {ECO:0000313|EMBL:AMM52501.1};
OS Rufibacter sp. DG15C.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM52501.1, ECO:0000313|Proteomes:UP000070672};
RN [1] {ECO:0000313|EMBL:AMM52501.1, ECO:0000313|Proteomes:UP000070672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG15C {ECO:0000313|EMBL:AMM52501.1,
RC ECO:0000313|Proteomes:UP000070672};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Rufibacter sp. DG15C whole genome sequencing.";
RL Submitted (JAN-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; CP010776; AMM52501.1; -; Genomic_DNA.
DR RefSeq; WP_066511843.1; NZ_CP010776.1.
DR AlphaFoldDB; A0A127B4Y3; -.
DR STRING; 1379909.TH61_16755; -.
DR KEGG; rud:TH61_16755; -.
DR PATRIC; fig|1379909.4.peg.3592; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000070672; Chromosome.
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; cd05799; PGM2; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000070672}.
FT DOMAIN 52..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..452
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 582 AA; 64732 MW; 42A25964FDEDDFA1 CRC64;
MENNLSLDAA VQAKLDTWLQ GGYDQETKAH LQQLMASQDT DTLTDCFYKD LEFGTGGLRG
IMGIGSNRMN RYTVGMATQG LSNYLLKSFP DQEVSVAIAH DSRNNSDVFA NVVADVFSGN
GIKVYFFKEL RPTPELSFAI RHLGCQSGVV LTASHNPKEY NGYKAYWNDG GQVTAPHDKN
IIAEVNKIQD LSQVKFTRDA SKIEYILEEV DEAYLDKVAR LSVDPAVIER QKDLKIVYTP
IHGTGITLVP RALERFGFTN VHVVEEQATP DGNFPTVVYP NPEEKEAMTL AMNKARELDA
DLVLATDPDA DRVGIAVKNH KGEFVLINGN QTAALLTYYV LSAWKKAGKL TGNEYIVSTI
VTTDLINRIA EGFGVDCYET LTGFKYIATI MREKEGQAQY ICGGEESYGF LVGDFVRDKD
AVSSCAMIAE MAASAKDQGK TLFELMIQMY QEFGFYKEDL ISITKKGHRG ALEIQEMMQE
LRENPPKTIA GSKVVEISDY KTGFRRNLLT REEHATGLES SNVLQYLTED GTKVSARPSG
TEPKIKFYFS VKEPLASAND FDKVSQQLEQ KIDAVITDLK LR
//
