ID A0A1B1BF21_9MICO Unreviewed; 538 AA.
AC A0A1B1BF21;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ANP71162.1};
GN ORFNames=PA27867_0188 {ECO:0000313|EMBL:ANP71162.1};
OS Cryobacterium arcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=670052 {ECO:0000313|EMBL:ANP71162.1, ECO:0000313|Proteomes:UP000092582};
RN [1] {ECO:0000313|EMBL:ANP71162.1, ECO:0000313|Proteomes:UP000092582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27867 {ECO:0000313|EMBL:ANP71162.1,
RC ECO:0000313|Proteomes:UP000092582};
RA Lee J., Kim O.-S.;
RT "Genome sequencing of Cryobacterium arcticum PAMC 27867.";
RL Submitted (JUN-2016) 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; CP016282; ANP71162.1; -; Genomic_DNA.
DR RefSeq; WP_066591936.1; NZ_CP016282.1.
DR AlphaFoldDB; A0A1B1BF21; -.
DR STRING; 670052.PA27867_0188; -.
DR KEGG; cart:PA27867_0188; -.
DR PATRIC; fig|670052.7.peg.200; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000092582; Chromosome 1.
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; 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 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}.
FT DOMAIN 38..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 204..308
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 314..432
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 538 AA; 57461 MW; 804F26B6C789E3A6 CRC64;
MNERAGTPAQ KSDLIDVEAL IRAYYDLKPD VSVPAQRVVF GTSGHRGSSL NTAFNENHIL
ATTQAIVEYR AGQGITGPLF IGADTHALSG PATTTALEVL VGNDVRVLVD EFDDYVPTPA
LSHAILAYNR AGHDDQADGI VVTPSHNPPM DGGFKYNPPH GGPADSDATS WIANRANEII
EGGMRDVRMS EPSAVETYDF RGHYVDDLEN IIDMKAIKAS GIRIGADPLG GASVGYWGAI
RDRYELNLTV VNPHVDPTWA FMTLDWDGKI RMDPSSPSAM ASVLAHKDEF DILTGNDADA
DRHGIVTPDA GLMNPNHFLA VAIEYLYSHR DGWRADAAIG KTLVSSTMID RVAGFLGREL
WEVPVGFKWF VPGLIDGSVA FGGEESAGAS FVRFDGTVWT TDKDGILLAL LASEIVAVTG
KSPSVRYAEL AEHFGAPAYE RIDAVATPAQ KAALSKLDGD AITATELAGD KIIGALSHAP
GNGAAIGGVK VFTEYAWFAA RPSGTEDVYK IYAESFKGPE HLKQVQIEAK AIVDAAIS
//
